Calcium in PDB 1cge: Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
Enzymatic activity of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
All present enzymatic activity of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself:
3.4.24.7;
Protein crystallography data
The structure of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself, PDB code: 1cge
was solved by
B.Lovejoy,
A.M.Hassell,
M.A.Luther,
D.Weigl,
S.R.Jordan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
7.00 /
1.90
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
72.600,
72.600,
75.100,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.8 /
n/a
|
Other elements in 1cge:
The structure of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
(pdb code 1cge). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the
Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself, PDB code: 1cge:
Jump to Calcium binding site number:
1;
2;
3;
Calcium binding site 1 out
of 3 in 1cge
Go back to
Calcium Binding Sites List in 1cge
Calcium binding site 1 out
of 3 in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca303
b:18.2
occ:1.00
|
OE2
|
A:GLU201
|
2.2
|
18.4
|
1.0
|
OD2
|
A:ASP198
|
2.3
|
15.8
|
1.0
|
O
|
A:GLY176
|
2.3
|
27.6
|
1.0
|
OD1
|
A:ASP175
|
2.3
|
28.3
|
1.0
|
O
|
A:ASN180
|
2.4
|
17.1
|
1.0
|
O
|
A:GLY178
|
2.4
|
20.7
|
1.0
|
CG
|
A:ASP198
|
3.4
|
14.1
|
1.0
|
H
|
A:ASP175
|
3.4
|
0.0
|
1.0
|
CD
|
A:GLU201
|
3.5
|
17.4
|
1.0
|
CG
|
A:ASP175
|
3.5
|
27.6
|
1.0
|
C
|
A:ASN180
|
3.5
|
17.1
|
1.0
|
C
|
A:GLY176
|
3.5
|
17.8
|
1.0
|
C
|
A:GLY178
|
3.6
|
17.1
|
1.0
|
H
|
A:GLY176
|
4.0
|
0.0
|
1.0
|
N
|
A:GLY176
|
4.0
|
17.4
|
1.0
|
CB
|
A:ASP198
|
4.0
|
14.4
|
1.0
|
N
|
A:GLY178
|
4.0
|
17.4
|
1.0
|
N
|
A:ASN180
|
4.0
|
18.7
|
1.0
|
H
|
A:ASN180
|
4.0
|
0.0
|
1.0
|
OD2
|
A:ASP175
|
4.1
|
28.7
|
1.0
|
C
|
A:PRO177
|
4.1
|
19.8
|
1.0
|
H
|
A:GLY178
|
4.2
|
0.0
|
1.0
|
C
|
A:ASP175
|
4.2
|
22.8
|
1.0
|
N
|
A:ASP175
|
4.2
|
24.6
|
1.0
|
OE1
|
A:GLU201
|
4.3
|
20.2
|
1.0
|
OD1
|
A:ASP198
|
4.3
|
15.1
|
1.0
|
CA
|
A:ASN180
|
4.3
|
18.0
|
1.0
|
CA
|
A:GLY176
|
4.4
|
16.7
|
1.0
|
C
|
A:GLY179
|
4.4
|
18.4
|
1.0
|
CG
|
A:GLU201
|
4.4
|
17.8
|
1.0
|
CA
|
A:GLY178
|
4.4
|
16.5
|
1.0
|
N
|
A:LEU181
|
4.4
|
14.8
|
1.0
|
N
|
A:PRO177
|
4.4
|
18.8
|
1.0
|
O
|
A:PRO177
|
4.4
|
24.2
|
1.0
|
CA
|
A:PRO177
|
4.5
|
19.3
|
1.0
|
CA
|
A:ASP175
|
4.5
|
24.1
|
1.0
|
CA
|
A:LEU181
|
4.6
|
12.6
|
1.0
|
CB
|
A:ASP175
|
4.6
|
26.7
|
1.0
|
N
|
A:GLY179
|
4.6
|
18.3
|
1.0
|
O
|
A:ASP175
|
4.6
|
24.9
|
1.0
|
CA
|
A:GLY179
|
4.7
|
18.9
|
1.0
|
CB
|
A:ASN180
|
4.8
|
22.0
|
1.0
|
H1
|
A:HOH542
|
4.8
|
0.0
|
1.0
|
O
|
A:GLY179
|
4.9
|
28.7
|
1.0
|
|
Calcium binding site 2 out
of 3 in 1cge
Go back to
Calcium Binding Sites List in 1cge
Calcium binding site 2 out
of 3 in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca304
b:21.9
occ:1.00
|
O
|
A:HOH600
|
2.2
|
27.0
|
1.0
|
OE2
|
A:GLU199
|
2.3
|
18.0
|
1.0
|
OD2
|
A:ASP124
|
2.3
|
24.1
|
1.0
|
O
|
A:HOH570
|
2.3
|
29.4
|
1.0
|
O
|
A:GLU199
|
2.4
|
16.8
|
1.0
|
OD1
|
A:ASP124
|
2.5
|
23.0
|
1.0
|
O
|
A:GLU201
|
2.6
|
19.1
|
1.0
|
H1
|
A:HOH600
|
2.6
|
0.0
|
1.0
|
H1
|
A:HOH570
|
2.7
|
0.0
|
1.0
|
CG
|
A:ASP124
|
2.8
|
22.4
|
1.0
|
H2
|
A:HOH600
|
2.9
|
0.0
|
1.0
|
H2
|
A:HOH570
|
2.9
|
0.0
|
1.0
|
HG1
|
A:THR122
|
3.4
|
0.0
|
1.0
|
CD
|
A:GLU199
|
3.4
|
16.5
|
1.0
|
C
|
A:GLU199
|
3.5
|
16.8
|
1.0
|
H1
|
A:HOH548
|
3.7
|
0.0
|
1.0
|
OG1
|
A:THR122
|
3.8
|
20.6
|
1.0
|
C
|
A:GLU201
|
3.8
|
11.7
|
1.0
|
H
|
A:TRP203
|
4.0
|
0.0
|
1.0
|
CG
|
A:GLU199
|
4.1
|
16.7
|
1.0
|
CA
|
A:GLU199
|
4.2
|
16.0
|
1.0
|
CB
|
A:ASP124
|
4.2
|
21.6
|
1.0
|
CD1
|
A:TRP203
|
4.3
|
11.5
|
1.0
|
CA
|
A:ARG202
|
4.4
|
13.3
|
1.0
|
H
|
A:ASP124
|
4.4
|
0.0
|
1.0
|
OE1
|
A:GLU199
|
4.4
|
17.9
|
1.0
|
N
|
A:GLU201
|
4.5
|
13.1
|
1.0
|
H
|
A:GLU201
|
4.6
|
0.0
|
1.0
|
N
|
A:ARG202
|
4.6
|
14.2
|
1.0
|
N
|
A:ASP200
|
4.6
|
21.6
|
1.0
|
HH22
|
A:ARG165
|
4.6
|
0.0
|
1.0
|
O
|
A:HOH569
|
4.6
|
32.7
|
1.0
|
C
|
A:ASP200
|
4.6
|
22.4
|
1.0
|
O
|
A:HOH548
|
4.7
|
31.0
|
1.0
|
N
|
A:TRP203
|
4.7
|
19.4
|
1.0
|
HE1
|
A:TRP203
|
4.7
|
0.0
|
1.0
|
CB
|
A:GLU199
|
4.7
|
14.4
|
1.0
|
CA
|
A:ASP200
|
4.8
|
21.7
|
1.0
|
CA
|
A:GLU201
|
4.8
|
12.0
|
1.0
|
NE1
|
A:TRP203
|
4.9
|
11.9
|
1.0
|
H2
|
A:HOH548
|
4.9
|
0.0
|
1.0
|
|
Calcium binding site 3 out
of 3 in 1cge
Go back to
Calcium Binding Sites List in 1cge
Calcium binding site 3 out
of 3 in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca305
b:20.1
occ:1.00
|
O
|
A:ASP158
|
2.3
|
18.5
|
1.0
|
O
|
A:HOH566
|
2.3
|
38.6
|
1.0
|
O
|
A:GLY192
|
2.3
|
11.3
|
1.0
|
O
|
A:HOH544
|
2.3
|
15.2
|
1.0
|
O
|
A:GLY190
|
2.4
|
18.2
|
1.0
|
OD1
|
A:ASP194
|
2.5
|
23.1
|
1.0
|
H1
|
A:HOH566
|
2.8
|
0.0
|
1.0
|
H2
|
A:HOH544
|
2.9
|
0.0
|
1.0
|
H1
|
A:HOH544
|
3.0
|
0.0
|
1.0
|
H2
|
A:HOH566
|
3.1
|
0.0
|
1.0
|
C
|
A:ASP158
|
3.4
|
13.9
|
1.0
|
CG
|
A:ASP194
|
3.4
|
20.9
|
1.0
|
C
|
A:GLY192
|
3.4
|
13.6
|
1.0
|
C
|
A:GLY190
|
3.6
|
16.8
|
1.0
|
H
|
A:MET160
|
3.8
|
0.0
|
1.0
|
OD2
|
A:ASP194
|
3.8
|
21.6
|
1.0
|
C
|
A:ILE191
|
3.8
|
20.7
|
1.0
|
H
|
A:ASP194
|
3.9
|
0.0
|
1.0
|
N
|
A:GLY192
|
4.0
|
17.7
|
1.0
|
H1
|
A:HOH546
|
4.0
|
0.0
|
1.0
|
O
|
A:ILE191
|
4.0
|
24.9
|
1.0
|
N
|
A:ASP194
|
4.1
|
16.2
|
1.0
|
CA
|
A:GLY192
|
4.2
|
14.1
|
1.0
|
O
|
A:HOH546
|
4.3
|
32.6
|
1.0
|
CA
|
A:ASP158
|
4.3
|
15.6
|
1.0
|
H
|
A:GLY192
|
4.3
|
0.0
|
1.0
|
CA
|
A:ILE191
|
4.3
|
22.8
|
1.0
|
N
|
A:ILE159
|
4.4
|
12.9
|
1.0
|
N
|
A:GLY193
|
4.4
|
8.2
|
1.0
|
N
|
A:ILE191
|
4.4
|
22.5
|
1.0
|
O
|
A:ALA157
|
4.5
|
19.8
|
1.0
|
O
|
A:GLY188
|
4.5
|
25.2
|
1.0
|
C
|
A:GLY193
|
4.5
|
10.7
|
1.0
|
CA
|
A:GLY193
|
4.5
|
9.4
|
1.0
|
CA
|
A:ILE159
|
4.5
|
13.8
|
1.0
|
O
|
A:HOH567
|
4.6
|
25.6
|
1.0
|
N
|
A:MET160
|
4.6
|
16.2
|
1.0
|
CA
|
A:GLY190
|
4.6
|
17.5
|
1.0
|
CB
|
A:ASP194
|
4.6
|
19.2
|
1.0
|
N
|
A:GLY190
|
4.6
|
17.8
|
1.0
|
CG
|
A:MET160
|
4.8
|
20.5
|
1.0
|
CA
|
A:ASP194
|
4.8
|
17.6
|
1.0
|
H
|
A:GLY190
|
4.9
|
0.0
|
1.0
|
C
|
A:PRO189
|
4.9
|
18.5
|
1.0
|
CH2
|
A:TRP109
|
4.9
|
15.7
|
1.0
|
H1
|
A:HOH567
|
4.9
|
0.0
|
1.0
|
|
Reference:
B.Lovejoy,
A.M.Hassell,
M.A.Luther,
D.Weigl,
S.R.Jordan.
Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself. Biochemistry V. 33 8207 1994.
ISSN: ISSN 0006-2960
PubMed: 8031754
DOI: 10.1021/BI00193A006
Page generated: Thu Jul 11 06:56:18 2024
|