Calcium in PDB 6eqx: X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba
Enzymatic activity of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba
All present enzymatic activity of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba:
3.4.21.75;
Protein crystallography data
The structure of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba, PDB code: 6eqx
was solved by
S.O.Dahms,
M.E.Than,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.16 /
1.99
|
Space group
|
P 65 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
131.805,
131.805,
155.347,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.2 /
18.4
|
Other elements in 6eqx:
The structure of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba
(pdb code 6eqx). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the
X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba, PDB code: 6eqx:
Jump to Calcium binding site number:
1;
2;
3;
Calcium binding site 1 out
of 3 in 6eqx
Go back to
Calcium Binding Sites List in 6eqx
Calcium binding site 1 out
of 3 in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca601
b:24.0
occ:1.00
|
OD2
|
A:ASP174
|
2.3
|
20.7
|
1.0
|
O
|
A:ASP181
|
2.4
|
20.1
|
1.0
|
O
|
A:HOH735
|
2.4
|
23.9
|
1.0
|
O
|
A:HOH814
|
2.4
|
25.2
|
1.0
|
O
|
A:HOH1081
|
2.5
|
24.9
|
1.0
|
OD2
|
A:ASP179
|
2.5
|
25.7
|
1.0
|
OD1
|
A:ASP179
|
2.6
|
24.0
|
1.0
|
CG
|
A:ASP179
|
2.9
|
24.9
|
1.0
|
CG
|
A:ASP174
|
3.3
|
20.9
|
1.0
|
CB
|
A:ASP174
|
3.5
|
20.9
|
1.0
|
C
|
A:ASP181
|
3.5
|
20.1
|
1.0
|
CB
|
A:ASP181
|
4.0
|
22.2
|
1.0
|
CA
|
A:ASP181
|
4.2
|
19.2
|
1.0
|
N
|
A:ASP181
|
4.3
|
22.3
|
1.0
|
CB
|
A:ASP179
|
4.4
|
23.4
|
1.0
|
OD1
|
A:ASP174
|
4.4
|
17.8
|
1.0
|
CG
|
A:ASP181
|
4.5
|
31.9
|
1.0
|
CB
|
A:ASP177
|
4.5
|
18.6
|
1.0
|
NH2
|
A:ARG225
|
4.5
|
24.9
|
1.0
|
OD2
|
A:ASP177
|
4.6
|
33.2
|
1.0
|
N
|
A:PRO182
|
4.6
|
21.9
|
1.0
|
N
|
A:GLN183
|
4.8
|
19.4
|
1.0
|
O
|
A:GLN183
|
4.8
|
17.9
|
1.0
|
CA
|
A:PRO182
|
4.8
|
18.4
|
1.0
|
O
|
A:HOH1120
|
4.9
|
43.4
|
1.0
|
OD1
|
A:ASP181
|
4.9
|
24.2
|
1.0
|
CD
|
A:ARG225
|
4.9
|
18.9
|
1.0
|
|
Calcium binding site 2 out
of 3 in 6eqx
Go back to
Calcium Binding Sites List in 6eqx
Calcium binding site 2 out
of 3 in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca602
b:22.3
occ:1.00
|
O
|
A:VAL205
|
2.3
|
24.1
|
1.0
|
O
|
A:VAL210
|
2.3
|
20.2
|
1.0
|
OD2
|
A:ASP115
|
2.4
|
22.1
|
1.0
|
O
|
A:GLY212
|
2.4
|
21.9
|
1.0
|
OD1
|
A:ASP162
|
2.4
|
22.5
|
1.0
|
OD1
|
A:ASN208
|
2.5
|
24.4
|
1.0
|
OD2
|
A:ASP162
|
2.6
|
22.9
|
1.0
|
CG
|
A:ASP162
|
2.8
|
23.5
|
1.0
|
CG
|
A:ASP115
|
3.5
|
22.2
|
1.0
|
C
|
A:VAL205
|
3.5
|
19.8
|
1.0
|
C
|
A:VAL210
|
3.5
|
26.3
|
1.0
|
CG
|
A:ASN208
|
3.5
|
23.8
|
1.0
|
C
|
A:GLY212
|
3.6
|
26.9
|
1.0
|
ND2
|
A:ASN208
|
3.9
|
19.7
|
1.0
|
CB
|
A:ASP115
|
4.1
|
23.8
|
1.0
|
N
|
A:GLY212
|
4.2
|
26.9
|
1.0
|
N
|
A:VAL210
|
4.3
|
25.4
|
1.0
|
CA
|
A:VAL210
|
4.3
|
24.3
|
1.0
|
C
|
A:CYS211
|
4.3
|
29.4
|
1.0
|
CB
|
A:ASP162
|
4.3
|
20.5
|
1.0
|
N
|
A:ALA206
|
4.4
|
21.6
|
1.0
|
N
|
A:VAL205
|
4.4
|
23.3
|
1.0
|
CB
|
A:VAL210
|
4.4
|
27.9
|
1.0
|
CA
|
A:ALA206
|
4.4
|
20.2
|
1.0
|
CA
|
A:GLY212
|
4.4
|
19.2
|
1.0
|
CA
|
A:VAL205
|
4.4
|
20.7
|
1.0
|
OD1
|
A:ASP115
|
4.5
|
22.1
|
1.0
|
N
|
A:CYS211
|
4.5
|
24.1
|
1.0
|
O
|
A:CYS211
|
4.5
|
22.7
|
1.0
|
N
|
A:VAL213
|
4.6
|
21.1
|
1.0
|
O
|
A:HOH864
|
4.6
|
20.5
|
1.0
|
CG1
|
A:VAL213
|
4.7
|
20.8
|
1.0
|
CA
|
A:VAL213
|
4.7
|
19.8
|
1.0
|
C
|
A:ALA206
|
4.7
|
24.3
|
1.0
|
CB
|
A:VAL205
|
4.8
|
23.8
|
1.0
|
N
|
A:ASN208
|
4.8
|
24.8
|
1.0
|
CA
|
A:CYS211
|
4.8
|
26.2
|
1.0
|
CB
|
A:ASN208
|
4.9
|
27.4
|
1.0
|
N
|
A:ASN207
|
4.9
|
26.4
|
1.0
|
C
|
A:ALA204
|
4.9
|
18.8
|
1.0
|
CB
|
A:CYS211
|
4.9
|
25.7
|
1.0
|
|
Calcium binding site 3 out
of 3 in 6eqx
Go back to
Calcium Binding Sites List in 6eqx
Calcium binding site 3 out
of 3 in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca603
b:15.3
occ:1.00
|
OD2
|
A:ASP301
|
2.3
|
14.8
|
1.0
|
O
|
A:HOH807
|
2.4
|
14.7
|
1.0
|
OD1
|
A:ASP258
|
2.4
|
18.7
|
1.0
|
OE1
|
A:GLU331
|
2.4
|
14.4
|
1.0
|
OE2
|
A:GLU331
|
2.5
|
16.7
|
1.0
|
O
|
A:HOH755
|
2.5
|
14.2
|
1.0
|
O
|
A:HOH976
|
2.5
|
16.1
|
1.0
|
CD
|
A:GLU331
|
2.8
|
15.6
|
1.0
|
CG
|
A:ASP301
|
3.3
|
18.0
|
1.0
|
CG
|
A:ASP258
|
3.5
|
20.6
|
1.0
|
OD1
|
A:ASP301
|
4.1
|
16.9
|
1.0
|
CB
|
A:ASP301
|
4.1
|
15.1
|
1.0
|
N35
|
D:00S6
|
4.1
|
14.8
|
1.0
|
CB
|
A:ASP258
|
4.2
|
18.0
|
1.0
|
CA
|
A:ASP258
|
4.2
|
17.5
|
1.0
|
CG
|
A:GLU331
|
4.3
|
16.1
|
1.0
|
O
|
A:HOH904
|
4.3
|
20.1
|
1.0
|
OD2
|
A:ASP258
|
4.4
|
17.9
|
1.0
|
O
|
A:SER302
|
4.4
|
17.6
|
1.0
|
OD2
|
A:ASP306
|
4.5
|
17.1
|
1.0
|
O
|
A:HOH925
|
4.5
|
16.7
|
1.0
|
O
|
A:SER293
|
4.5
|
17.3
|
1.0
|
CA
|
A:GLY294
|
4.6
|
13.1
|
1.0
|
O
|
A:GLU257
|
4.6
|
17.3
|
1.0
|
CB
|
A:ASP306
|
4.7
|
14.1
|
1.0
|
CA
|
A:CYS303
|
4.8
|
15.0
|
1.0
|
C27
|
D:00S6
|
4.8
|
17.4
|
1.0
|
N
|
A:GLY296
|
4.8
|
18.6
|
1.0
|
C
|
A:SER302
|
4.8
|
16.5
|
1.0
|
O
|
A:PRO256
|
4.9
|
15.7
|
1.0
|
N
|
A:ASP258
|
5.0
|
18.6
|
1.0
|
CA
|
A:GLY296
|
5.0
|
15.2
|
1.0
|
|
Reference:
S.O.Dahms,
K.Hardes,
T.Steinmetzer,
M.E.Than.
X-Ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants Beyond the S4 Pocket. Biochemistry V. 57 925 2018.
ISSN: ISSN 1520-4995
PubMed: 29314830
DOI: 10.1021/ACS.BIOCHEM.7B01124
Page generated: Sat Dec 12 06:05:23 2020
|