Calcium in PDB 1p8j: Crystal Structure of the Proprotein Convertase Furin
Enzymatic activity of Crystal Structure of the Proprotein Convertase Furin
All present enzymatic activity of Crystal Structure of the Proprotein Convertase Furin:
3.4.21.75;
Protein crystallography data
The structure of Crystal Structure of the Proprotein Convertase Furin, PDB code: 1p8j
was solved by
S.Henrich,
A.Cameron,
G.P.Bourenkov,
R.Kiefersauer,
R.Huber,
I.Lindberg,
W.Bode,
M.E.Than,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
18.82 /
2.60
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.305,
135.392,
137.806,
103.56,
98.98,
107.09
|
R / Rfree (%)
|
18.8 /
21.9
|
Calcium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
16;
Binding sites:
The binding sites of Calcium atom in the Crystal Structure of the Proprotein Convertase Furin
(pdb code 1p8j). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 16 binding sites of Calcium where determined in the
Crystal Structure of the Proprotein Convertase Furin, PDB code: 1p8j:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Calcium binding site 1 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 1 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca3001
b:17.2
occ:1.00
|
O
|
A:VAL205
|
2.2
|
19.6
|
1.0
|
O
|
A:GLY212
|
2.3
|
17.7
|
1.0
|
O
|
A:VAL210
|
2.3
|
22.6
|
1.0
|
OD1
|
A:ASP115
|
2.4
|
23.8
|
1.0
|
OD1
|
A:ASP162
|
2.4
|
22.4
|
1.0
|
OD1
|
A:ASN208
|
2.6
|
24.3
|
1.0
|
OD2
|
A:ASP162
|
2.8
|
22.0
|
1.0
|
CG
|
A:ASP162
|
2.9
|
21.6
|
1.0
|
CG
|
A:ASP115
|
3.4
|
23.6
|
1.0
|
C
|
A:VAL205
|
3.4
|
20.3
|
1.0
|
C
|
A:GLY212
|
3.5
|
18.6
|
1.0
|
C
|
A:VAL210
|
3.5
|
23.9
|
1.0
|
CG
|
A:ASN208
|
3.6
|
24.3
|
1.0
|
ND2
|
A:ASN208
|
4.0
|
24.4
|
1.0
|
N
|
A:GLY212
|
4.1
|
21.5
|
1.0
|
CB
|
A:ASP115
|
4.1
|
23.8
|
1.0
|
N
|
A:VAL210
|
4.2
|
25.7
|
1.0
|
CA
|
A:VAL210
|
4.2
|
24.7
|
1.0
|
CA
|
A:GLY212
|
4.3
|
18.9
|
1.0
|
C
|
A:CYS211
|
4.3
|
24.3
|
1.0
|
OD2
|
A:ASP115
|
4.3
|
24.7
|
1.0
|
N
|
A:ALA206
|
4.3
|
21.4
|
1.0
|
CA
|
A:ALA206
|
4.3
|
21.8
|
1.0
|
CB
|
A:VAL210
|
4.4
|
25.3
|
1.0
|
CA
|
A:VAL205
|
4.4
|
19.9
|
1.0
|
CB
|
A:ASP162
|
4.4
|
21.5
|
1.0
|
N
|
A:VAL213
|
4.5
|
17.9
|
1.0
|
N
|
A:VAL205
|
4.5
|
19.0
|
1.0
|
N
|
A:CYS211
|
4.5
|
24.5
|
1.0
|
CG1
|
A:VAL213
|
4.6
|
19.0
|
1.0
|
CA
|
A:VAL213
|
4.6
|
18.2
|
1.0
|
O
|
A:CYS211
|
4.6
|
25.4
|
1.0
|
O
|
A:HOH4114
|
4.7
|
14.7
|
1.0
|
CB
|
A:VAL205
|
4.7
|
20.4
|
1.0
|
N
|
A:ASN208
|
4.8
|
23.0
|
1.0
|
CA
|
A:CYS211
|
4.8
|
25.9
|
1.0
|
C
|
A:ALA206
|
4.8
|
22.1
|
1.0
|
CB
|
A:CYS211
|
4.9
|
28.1
|
1.0
|
C
|
A:ALA204
|
4.9
|
19.1
|
1.0
|
CB
|
A:ASN208
|
4.9
|
23.4
|
1.0
|
N
|
A:ASN207
|
4.9
|
22.4
|
1.0
|
|
Calcium binding site 2 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 2 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca3002
b:7.6
occ:1.00
|
OD1
|
A:ASP258
|
2.2
|
13.0
|
1.0
|
OE1
|
A:GLU331
|
2.3
|
15.6
|
1.0
|
O
|
A:HOH4270
|
2.3
|
5.2
|
1.0
|
O
|
A:HOH4271
|
2.3
|
3.5
|
1.0
|
OD1
|
A:ASP301
|
2.4
|
14.4
|
1.0
|
O
|
A:HOH4269
|
2.4
|
8.9
|
1.0
|
OE2
|
A:GLU331
|
2.5
|
15.1
|
1.0
|
CD
|
A:GLU331
|
2.7
|
15.2
|
1.0
|
CG
|
A:ASP301
|
3.3
|
17.0
|
1.0
|
CG
|
A:ASP258
|
3.3
|
14.6
|
1.0
|
NH1
|
J:AR7805
|
3.9
|
15.4
|
1.0
|
OD2
|
A:ASP301
|
4.0
|
18.1
|
1.0
|
CB
|
A:ASP258
|
4.0
|
14.9
|
1.0
|
CB
|
A:ASP301
|
4.1
|
16.1
|
1.0
|
CA
|
A:ASP258
|
4.1
|
15.2
|
1.0
|
CG
|
A:GLU331
|
4.2
|
13.8
|
1.0
|
OD2
|
A:ASP258
|
4.2
|
13.5
|
1.0
|
O
|
A:HOH4138
|
4.2
|
10.0
|
1.0
|
CA
|
A:GLY294
|
4.4
|
14.6
|
1.0
|
O
|
A:SER293
|
4.4
|
15.2
|
1.0
|
O
|
A:HOH4081
|
4.5
|
15.6
|
1.0
|
O
|
A:SER302
|
4.6
|
20.8
|
1.0
|
OD2
|
A:ASP306
|
4.6
|
10.0
|
1.0
|
CZ
|
J:AR7805
|
4.6
|
15.1
|
1.0
|
O
|
A:GLU257
|
4.7
|
12.7
|
1.0
|
CB
|
A:ASP306
|
4.7
|
12.1
|
1.0
|
CA
|
A:CYS303
|
4.8
|
20.4
|
1.0
|
N
|
A:GLY296
|
4.8
|
17.5
|
1.0
|
O
|
A:PRO256
|
4.9
|
14.4
|
1.0
|
C
|
A:SER302
|
4.9
|
19.6
|
1.0
|
N
|
A:ASP258
|
5.0
|
14.8
|
1.0
|
N
|
A:CYS303
|
5.0
|
19.2
|
1.0
|
|
Calcium binding site 3 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 3 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca3003
b:18.4
occ:1.00
|
O
|
B:VAL205
|
2.2
|
22.4
|
1.0
|
O
|
B:VAL210
|
2.3
|
25.6
|
1.0
|
OD1
|
B:ASP162
|
2.4
|
24.2
|
1.0
|
O
|
B:GLY212
|
2.4
|
20.6
|
1.0
|
OD1
|
B:ASP115
|
2.4
|
26.4
|
1.0
|
OD1
|
B:ASN208
|
2.5
|
25.9
|
1.0
|
OD2
|
B:ASP162
|
2.8
|
21.5
|
1.0
|
CG
|
B:ASP162
|
2.9
|
21.5
|
1.0
|
C
|
B:VAL205
|
3.4
|
22.3
|
1.0
|
CG
|
B:ASN208
|
3.4
|
25.8
|
1.0
|
CG
|
B:ASP115
|
3.4
|
26.2
|
1.0
|
C
|
B:VAL210
|
3.5
|
26.2
|
1.0
|
C
|
B:GLY212
|
3.6
|
21.7
|
1.0
|
ND2
|
B:ASN208
|
3.8
|
26.6
|
1.0
|
CB
|
B:ASP115
|
4.1
|
25.5
|
1.0
|
N
|
B:VAL210
|
4.1
|
26.8
|
1.0
|
N
|
B:GLY212
|
4.1
|
24.2
|
1.0
|
CA
|
B:VAL210
|
4.2
|
25.6
|
1.0
|
C
|
B:CYS211
|
4.3
|
25.6
|
1.0
|
CB
|
B:VAL210
|
4.3
|
25.6
|
1.0
|
N
|
B:ALA206
|
4.3
|
22.4
|
1.0
|
CA
|
B:ALA206
|
4.4
|
22.6
|
1.0
|
CA
|
B:GLY212
|
4.4
|
22.5
|
1.0
|
OD2
|
B:ASP115
|
4.4
|
24.8
|
1.0
|
CA
|
B:VAL205
|
4.4
|
22.4
|
1.0
|
CB
|
B:ASP162
|
4.4
|
20.9
|
1.0
|
N
|
B:VAL205
|
4.5
|
21.7
|
1.0
|
N
|
B:CYS211
|
4.5
|
26.7
|
1.0
|
N
|
B:VAL213
|
4.6
|
20.4
|
1.0
|
O
|
B:CYS211
|
4.6
|
26.1
|
1.0
|
CG1
|
B:VAL213
|
4.6
|
20.3
|
1.0
|
N
|
B:ASN208
|
4.7
|
24.9
|
1.0
|
CB
|
B:VAL205
|
4.7
|
22.3
|
1.0
|
CA
|
B:VAL213
|
4.7
|
20.4
|
1.0
|
CB
|
B:ASN208
|
4.7
|
24.4
|
1.0
|
C
|
B:ALA206
|
4.8
|
23.2
|
1.0
|
CA
|
B:CYS211
|
4.8
|
26.3
|
1.0
|
CB
|
B:CYS211
|
4.9
|
28.0
|
1.0
|
N
|
B:ASN207
|
4.9
|
23.2
|
1.0
|
C
|
B:ALA204
|
4.9
|
21.7
|
1.0
|
CG1
|
B:VAL210
|
4.9
|
25.2
|
1.0
|
|
Calcium binding site 4 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 4 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca3004
b:11.2
occ:1.00
|
OD1
|
B:ASP258
|
2.2
|
12.3
|
1.0
|
O
|
B:HOH4199
|
2.2
|
1.9
|
1.0
|
OE1
|
B:GLU331
|
2.3
|
12.5
|
1.0
|
OD1
|
B:ASP301
|
2.4
|
14.9
|
1.0
|
O
|
B:HOH4248
|
2.4
|
4.5
|
1.0
|
O
|
B:HOH4258
|
2.4
|
9.3
|
1.0
|
OE2
|
B:GLU331
|
2.4
|
10.5
|
1.0
|
CD
|
B:GLU331
|
2.6
|
12.4
|
1.0
|
CG
|
B:ASP301
|
3.3
|
14.3
|
1.0
|
CG
|
B:ASP258
|
3.3
|
17.0
|
1.0
|
OD2
|
B:ASP301
|
4.0
|
14.6
|
1.0
|
CB
|
B:ASP258
|
4.0
|
16.5
|
1.0
|
CB
|
B:ASP301
|
4.1
|
16.5
|
1.0
|
NH1
|
K:AR7805
|
4.1
|
11.5
|
1.0
|
CA
|
B:ASP258
|
4.1
|
16.9
|
1.0
|
CG
|
B:GLU331
|
4.1
|
12.6
|
1.0
|
OD2
|
B:ASP258
|
4.2
|
16.9
|
1.0
|
CA
|
B:GLY294
|
4.4
|
15.3
|
1.0
|
O
|
B:SER293
|
4.4
|
16.1
|
1.0
|
O
|
B:SER302
|
4.5
|
20.2
|
1.0
|
O
|
B:HOH4200
|
4.6
|
12.2
|
1.0
|
O
|
B:HOH4074
|
4.6
|
9.8
|
1.0
|
OD2
|
B:ASP306
|
4.7
|
8.2
|
1.0
|
O
|
B:GLU257
|
4.7
|
14.4
|
1.0
|
CA
|
B:CYS303
|
4.7
|
19.2
|
1.0
|
CB
|
B:ASP306
|
4.8
|
11.1
|
1.0
|
CZ
|
K:AR7805
|
4.8
|
13.1
|
1.0
|
N
|
B:GLY296
|
4.8
|
17.0
|
1.0
|
C
|
B:SER302
|
4.8
|
20.1
|
1.0
|
O
|
B:PRO256
|
5.0
|
12.4
|
1.0
|
N
|
B:CYS303
|
5.0
|
20.1
|
1.0
|
N
|
B:ASP258
|
5.0
|
16.0
|
1.0
|
CB
|
B:GLU331
|
5.0
|
14.4
|
1.0
|
|
Calcium binding site 5 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 5 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca3005
b:21.5
occ:1.00
|
O
|
C:VAL210
|
2.2
|
22.2
|
1.0
|
O
|
C:VAL205
|
2.3
|
18.4
|
1.0
|
O
|
C:GLY212
|
2.3
|
19.7
|
1.0
|
OD1
|
C:ASP115
|
2.4
|
25.8
|
1.0
|
OD1
|
C:ASP162
|
2.4
|
20.6
|
1.0
|
OD1
|
C:ASN208
|
2.5
|
24.7
|
1.0
|
OD2
|
C:ASP162
|
2.7
|
22.8
|
1.0
|
CG
|
C:ASP162
|
2.9
|
21.5
|
1.0
|
C
|
C:VAL210
|
3.4
|
23.4
|
1.0
|
CG
|
C:ASP115
|
3.4
|
24.5
|
1.0
|
C
|
C:VAL205
|
3.5
|
20.2
|
1.0
|
C
|
C:GLY212
|
3.5
|
19.1
|
1.0
|
CG
|
C:ASN208
|
3.5
|
23.4
|
1.0
|
ND2
|
C:ASN208
|
3.9
|
23.5
|
1.0
|
N
|
C:GLY212
|
4.1
|
21.6
|
1.0
|
CB
|
C:ASP115
|
4.1
|
23.9
|
1.0
|
N
|
C:VAL210
|
4.1
|
23.8
|
1.0
|
CA
|
C:VAL210
|
4.1
|
22.6
|
1.0
|
C
|
C:CYS211
|
4.3
|
24.2
|
1.0
|
CB
|
C:VAL210
|
4.3
|
22.8
|
1.0
|
CA
|
C:GLY212
|
4.3
|
18.9
|
1.0
|
N
|
C:ALA206
|
4.4
|
20.9
|
1.0
|
OD2
|
C:ASP115
|
4.4
|
23.0
|
1.0
|
CB
|
C:ASP162
|
4.4
|
20.6
|
1.0
|
CA
|
C:ALA206
|
4.4
|
22.0
|
1.0
|
CA
|
C:VAL205
|
4.5
|
19.6
|
1.0
|
N
|
C:CYS211
|
4.5
|
23.4
|
1.0
|
N
|
C:VAL205
|
4.5
|
19.4
|
1.0
|
N
|
C:VAL213
|
4.5
|
18.4
|
1.0
|
O
|
C:HOH4116
|
4.6
|
12.8
|
1.0
|
CG1
|
C:VAL213
|
4.6
|
17.7
|
1.0
|
O
|
C:CYS211
|
4.6
|
24.9
|
1.0
|
CA
|
C:VAL213
|
4.7
|
18.2
|
1.0
|
CA
|
C:CYS211
|
4.7
|
24.8
|
1.0
|
N
|
C:ASN208
|
4.8
|
23.3
|
1.0
|
CB
|
C:CYS211
|
4.8
|
27.3
|
1.0
|
CB
|
C:VAL205
|
4.8
|
19.0
|
1.0
|
C
|
C:ALA206
|
4.8
|
21.9
|
1.0
|
CB
|
C:ASN208
|
4.9
|
22.8
|
1.0
|
C
|
C:ALA204
|
4.9
|
18.6
|
1.0
|
N
|
C:ASN207
|
4.9
|
23.1
|
1.0
|
CG1
|
C:VAL210
|
4.9
|
20.9
|
1.0
|
|
Calcium binding site 6 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 6 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 6 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca3006
b:10.1
occ:1.00
|
O
|
C:HOH4135
|
2.2
|
6.7
|
1.0
|
OE1
|
C:GLU331
|
2.3
|
15.4
|
1.0
|
OD1
|
C:ASP258
|
2.3
|
14.9
|
1.0
|
OD1
|
C:ASP301
|
2.4
|
15.6
|
1.0
|
O
|
C:HOH4102
|
2.4
|
11.6
|
1.0
|
O
|
C:HOH4063
|
2.4
|
0.8
|
1.0
|
OE2
|
C:GLU331
|
2.5
|
12.4
|
1.0
|
CD
|
C:GLU331
|
2.7
|
14.5
|
1.0
|
CG
|
C:ASP301
|
3.3
|
17.6
|
1.0
|
CG
|
C:ASP258
|
3.4
|
15.8
|
1.0
|
OD2
|
C:ASP301
|
4.0
|
20.4
|
1.0
|
CB
|
C:ASP258
|
4.0
|
15.1
|
1.0
|
NH1
|
L:AR7805
|
4.1
|
15.4
|
1.0
|
CB
|
C:ASP301
|
4.1
|
17.4
|
1.0
|
CA
|
C:ASP258
|
4.2
|
15.4
|
1.0
|
CG
|
C:GLU331
|
4.2
|
13.0
|
1.0
|
OD2
|
C:ASP258
|
4.3
|
14.7
|
1.0
|
O
|
C:SER293
|
4.4
|
17.4
|
1.0
|
CA
|
C:GLY294
|
4.4
|
14.2
|
1.0
|
O
|
C:HOH4263
|
4.4
|
16.4
|
1.0
|
O
|
C:HOH4134
|
4.5
|
7.5
|
1.0
|
O
|
C:SER302
|
4.5
|
20.6
|
1.0
|
OD2
|
C:ASP306
|
4.6
|
9.3
|
1.0
|
O
|
C:GLU257
|
4.6
|
13.2
|
1.0
|
CB
|
C:ASP306
|
4.7
|
11.7
|
1.0
|
CA
|
C:CYS303
|
4.7
|
20.7
|
1.0
|
CZ
|
L:AR7805
|
4.7
|
14.2
|
1.0
|
C
|
C:SER302
|
4.8
|
20.1
|
1.0
|
N
|
C:GLY296
|
4.8
|
15.4
|
1.0
|
O
|
C:PRO256
|
4.9
|
14.2
|
1.0
|
N
|
C:CYS303
|
4.9
|
20.2
|
1.0
|
|
Calcium binding site 7 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 7 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 7 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca3007
b:29.7
occ:1.00
|
O
|
D:VAL205
|
2.2
|
22.8
|
1.0
|
O
|
D:VAL210
|
2.3
|
27.0
|
1.0
|
O
|
D:GLY212
|
2.3
|
26.2
|
1.0
|
OD1
|
D:ASP162
|
2.3
|
28.2
|
1.0
|
OD1
|
D:ASP115
|
2.4
|
30.2
|
1.0
|
OD1
|
D:ASN208
|
2.6
|
28.4
|
1.0
|
OD2
|
D:ASP162
|
2.7
|
28.7
|
1.0
|
CG
|
D:ASP162
|
2.9
|
27.3
|
1.0
|
C
|
D:VAL205
|
3.4
|
24.3
|
1.0
|
CG
|
D:ASP115
|
3.4
|
29.5
|
1.0
|
C
|
D:VAL210
|
3.5
|
28.0
|
1.0
|
C
|
D:GLY212
|
3.5
|
24.5
|
1.0
|
CG
|
D:ASN208
|
3.5
|
28.8
|
1.0
|
ND2
|
D:ASN208
|
3.9
|
28.7
|
1.0
|
N
|
D:GLY212
|
4.1
|
26.5
|
1.0
|
CB
|
D:ASP115
|
4.1
|
28.5
|
1.0
|
N
|
D:VAL210
|
4.2
|
28.3
|
1.0
|
CA
|
D:VAL210
|
4.2
|
28.0
|
1.0
|
N
|
D:ALA206
|
4.3
|
25.2
|
1.0
|
CA
|
D:ALA206
|
4.3
|
25.5
|
1.0
|
C
|
D:CYS211
|
4.3
|
27.6
|
1.0
|
CA
|
D:GLY212
|
4.3
|
24.6
|
1.0
|
CB
|
D:VAL210
|
4.3
|
28.2
|
1.0
|
OD2
|
D:ASP115
|
4.3
|
29.4
|
1.0
|
CA
|
D:VAL205
|
4.3
|
23.8
|
1.0
|
CB
|
D:ASP162
|
4.4
|
25.9
|
1.0
|
N
|
D:VAL205
|
4.4
|
23.5
|
1.0
|
CG1
|
D:VAL213
|
4.5
|
22.4
|
1.0
|
N
|
D:VAL213
|
4.5
|
23.3
|
1.0
|
N
|
D:CYS211
|
4.5
|
28.6
|
1.0
|
O
|
D:CYS211
|
4.6
|
27.8
|
1.0
|
CA
|
D:VAL213
|
4.6
|
22.5
|
1.0
|
CB
|
D:VAL205
|
4.7
|
23.0
|
1.0
|
C
|
D:ALA206
|
4.8
|
25.7
|
1.0
|
N
|
D:ASN208
|
4.8
|
26.5
|
1.0
|
CA
|
D:CYS211
|
4.8
|
28.9
|
1.0
|
CB
|
D:ASN208
|
4.8
|
27.8
|
1.0
|
C
|
D:ALA204
|
4.8
|
23.4
|
1.0
|
CB
|
D:CYS211
|
4.8
|
31.6
|
1.0
|
CG1
|
D:VAL210
|
4.9
|
25.9
|
1.0
|
N
|
D:ASN207
|
4.9
|
26.5
|
1.0
|
|
Calcium binding site 8 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 8 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 8 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca3008
b:16.6
occ:1.00
|
O
|
D:HOH4160
|
2.3
|
13.3
|
1.0
|
OD1
|
D:ASP258
|
2.3
|
20.0
|
1.0
|
OE1
|
D:GLU331
|
2.3
|
15.6
|
1.0
|
O
|
D:HOH4192
|
2.3
|
12.8
|
1.0
|
OD1
|
D:ASP301
|
2.3
|
19.4
|
1.0
|
O
|
D:HOH4070
|
2.4
|
10.8
|
1.0
|
OE2
|
D:GLU331
|
2.4
|
13.8
|
1.0
|
CD
|
D:GLU331
|
2.7
|
15.4
|
1.0
|
CG
|
D:ASP301
|
3.2
|
18.3
|
1.0
|
CG
|
D:ASP258
|
3.4
|
19.9
|
1.0
|
OD2
|
D:ASP301
|
3.9
|
18.3
|
1.0
|
CB
|
D:ASP258
|
4.1
|
18.6
|
1.0
|
CB
|
D:ASP301
|
4.1
|
19.1
|
1.0
|
CA
|
D:ASP258
|
4.1
|
18.7
|
1.0
|
NH1
|
M:AR7805
|
4.2
|
16.1
|
1.0
|
CG
|
D:GLU331
|
4.2
|
15.5
|
1.0
|
OD2
|
D:ASP258
|
4.4
|
19.8
|
1.0
|
O
|
D:SER302
|
4.4
|
20.3
|
1.0
|
O
|
D:SER293
|
4.5
|
18.9
|
1.0
|
CA
|
D:GLY294
|
4.5
|
17.6
|
1.0
|
O
|
D:GLU257
|
4.7
|
16.8
|
1.0
|
OD2
|
D:ASP306
|
4.7
|
15.6
|
1.0
|
CB
|
D:ASP306
|
4.7
|
14.6
|
1.0
|
CA
|
D:CYS303
|
4.7
|
21.0
|
1.0
|
C
|
D:SER302
|
4.8
|
20.7
|
1.0
|
CZ
|
M:AR7805
|
4.8
|
16.7
|
1.0
|
O
|
D:PRO256
|
4.9
|
17.9
|
1.0
|
N
|
D:GLY296
|
4.9
|
18.8
|
1.0
|
N
|
D:CYS303
|
4.9
|
21.4
|
1.0
|
N
|
D:ASP258
|
5.0
|
18.4
|
1.0
|
|
Calcium binding site 9 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 9 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 9 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca3009
b:22.0
occ:1.00
|
O
|
E:VAL205
|
2.2
|
20.6
|
1.0
|
O
|
E:GLY212
|
2.3
|
17.8
|
1.0
|
O
|
E:VAL210
|
2.3
|
21.7
|
1.0
|
OD1
|
E:ASP162
|
2.4
|
25.8
|
1.0
|
OD1
|
E:ASP115
|
2.4
|
28.1
|
1.0
|
OD1
|
E:ASN208
|
2.6
|
28.3
|
1.0
|
OD2
|
E:ASP162
|
2.8
|
24.8
|
1.0
|
CG
|
E:ASP162
|
2.9
|
24.4
|
1.0
|
CG
|
E:ASP115
|
3.4
|
26.1
|
1.0
|
C
|
E:VAL205
|
3.4
|
21.3
|
1.0
|
C
|
E:GLY212
|
3.5
|
18.9
|
1.0
|
C
|
E:VAL210
|
3.5
|
23.1
|
1.0
|
CG
|
E:ASN208
|
3.6
|
26.8
|
1.0
|
ND2
|
E:ASN208
|
4.0
|
28.0
|
1.0
|
N
|
E:GLY212
|
4.1
|
21.8
|
1.0
|
CB
|
E:ASP115
|
4.1
|
24.9
|
1.0
|
N
|
E:VAL210
|
4.2
|
24.2
|
1.0
|
CA
|
E:VAL210
|
4.2
|
23.6
|
1.0
|
CA
|
E:GLY212
|
4.3
|
19.0
|
1.0
|
N
|
E:ALA206
|
4.3
|
22.4
|
1.0
|
CA
|
E:ALA206
|
4.3
|
23.3
|
1.0
|
OD2
|
E:ASP115
|
4.3
|
26.3
|
1.0
|
C
|
E:CYS211
|
4.3
|
24.1
|
1.0
|
CB
|
E:VAL210
|
4.4
|
23.2
|
1.0
|
CA
|
E:VAL205
|
4.4
|
20.8
|
1.0
|
CB
|
E:ASP162
|
4.4
|
22.6
|
1.0
|
N
|
E:VAL213
|
4.5
|
18.5
|
1.0
|
N
|
E:VAL205
|
4.5
|
21.0
|
1.0
|
CG1
|
E:VAL213
|
4.5
|
18.8
|
1.0
|
O
|
E:HOH4147
|
4.5
|
11.4
|
1.0
|
N
|
E:CYS211
|
4.6
|
23.3
|
1.0
|
CA
|
E:VAL213
|
4.6
|
18.7
|
1.0
|
O
|
E:CYS211
|
4.7
|
23.5
|
1.0
|
CB
|
E:VAL205
|
4.7
|
20.9
|
1.0
|
C
|
E:ALA206
|
4.8
|
24.1
|
1.0
|
N
|
E:ASN208
|
4.8
|
24.8
|
1.0
|
CA
|
E:CYS211
|
4.8
|
25.0
|
1.0
|
C
|
E:ALA204
|
4.9
|
20.5
|
1.0
|
CB
|
E:CYS211
|
4.9
|
27.5
|
1.0
|
N
|
E:ASN207
|
4.9
|
24.4
|
1.0
|
CB
|
E:ASN208
|
4.9
|
24.8
|
1.0
|
CB
|
E:ALA204
|
5.0
|
16.8
|
1.0
|
|
Calcium binding site 10 out
of 16 in 1p8j
Go back to
Calcium Binding Sites List in 1p8j
Calcium binding site 10 out
of 16 in the Crystal Structure of the Proprotein Convertase Furin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 10 of Crystal Structure of the Proprotein Convertase Furin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca3010
b:9.8
occ:1.00
|
OD1
|
E:ASP258
|
2.2
|
16.5
|
1.0
|
OE1
|
E:GLU331
|
2.2
|
13.1
|
1.0
|
O
|
E:HOH4104
|
2.3
|
4.7
|
1.0
|
O
|
E:HOH4253
|
2.3
|
5.1
|
1.0
|
O
|
E:HOH4252
|
2.3
|
7.8
|
1.0
|
OD1
|
E:ASP301
|
2.4
|
17.0
|
1.0
|
OE2
|
E:GLU331
|
2.5
|
10.9
|
1.0
|
CD
|
E:GLU331
|
2.7
|
13.3
|
1.0
|
CG
|
E:ASP258
|
3.3
|
16.9
|
1.0
|
CG
|
E:ASP301
|
3.3
|
18.5
|
1.0
|
NH1
|
N:AR7805
|
3.9
|
9.1
|
1.0
|
CB
|
E:ASP258
|
4.1
|
15.4
|
1.0
|
OD2
|
E:ASP301
|
4.1
|
18.7
|
1.0
|
OD2
|
E:ASP258
|
4.2
|
15.3
|
1.0
|
CA
|
E:ASP258
|
4.2
|
15.4
|
1.0
|
CB
|
E:ASP301
|
4.2
|
18.3
|
1.0
|
CG
|
E:GLU331
|
4.2
|
12.1
|
1.0
|
O
|
E:SER293
|
4.3
|
15.8
|
1.0
|
CA
|
E:GLY294
|
4.3
|
12.9
|
1.0
|
O
|
E:HOH4083
|
4.5
|
5.9
|
1.0
|
OD2
|
E:ASP306
|
4.5
|
13.2
|
1.0
|
O
|
E:SER302
|
4.5
|
20.7
|
1.0
|
CZ
|
N:AR7805
|
4.6
|
10.3
|
1.0
|
CB
|
E:ASP306
|
4.7
|
13.0
|
1.0
|
O
|
E:GLU257
|
4.7
|
13.8
|
1.0
|
CA
|
E:CYS303
|
4.7
|
19.3
|
1.0
|
O
|
E:PRO256
|
4.8
|
14.9
|
1.0
|
N
|
E:GLY296
|
4.9
|
17.1
|
1.0
|
C
|
E:SER302
|
4.9
|
18.9
|
1.0
|
N
|
E:CYS303
|
5.0
|
18.3
|
1.0
|
C
|
E:GLY294
|
5.0
|
14.6
|
1.0
|
|
Reference:
S.Henrich,
A.Cameron,
G.P.Bourenkov,
R.Kiefersauer,
R.Huber,
I.Lindberg,
W.Bode,
M.E.Than.
The Crystal Structure of the Proprotein Processing Proteinase Furin Explains Its Stringent Specificity Nat.Struct.Biol. V. 10 520 2003.
ISSN: ISSN 1072-8368
PubMed: 12794637
DOI: 10.1038/NSB941
Page generated: Thu Jul 11 13:40:16 2024
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