Zinc in PDB 1cqr: Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
Enzymatic activity of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
All present enzymatic activity of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution:
3.4.24.17;
Protein crystallography data
The structure of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution, PDB code: 1cqr
was solved by
L.Chen,
T.J.Rydel,
F.Gu,
C.M.Dunaway,
S.Pikul,
K.M.Dunham,
B.L.Barnett,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
12.00 /
2.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
38.200,
79.100,
107.400,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.9 /
26.6
|
Other elements in 1cqr:
The structure of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
(pdb code 1cqr). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution, PDB code: 1cqr:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1cqr
Go back to
Zinc Binding Sites List in 1cqr
Zinc binding site 1 out
of 4 in the Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1301
b:12.6
occ:1.00
|
NE2
|
A:HIS201
|
2.1
|
9.6
|
1.0
|
NE2
|
A:HIS211
|
2.2
|
16.5
|
1.0
|
NE2
|
A:HIS205
|
2.2
|
7.2
|
1.0
|
CD2
|
A:HIS201
|
3.0
|
9.8
|
1.0
|
CE1
|
A:HIS211
|
3.0
|
18.7
|
1.0
|
CD2
|
A:HIS205
|
3.1
|
6.1
|
1.0
|
CD2
|
A:HIS211
|
3.1
|
16.8
|
1.0
|
CE1
|
A:HIS205
|
3.1
|
4.4
|
1.0
|
CE1
|
A:HIS201
|
3.2
|
8.9
|
1.0
|
ND1
|
A:HIS211
|
4.1
|
19.1
|
1.0
|
CG
|
A:HIS201
|
4.2
|
8.9
|
1.0
|
O
|
A:HOH14
|
4.2
|
24.7
|
1.0
|
CG
|
A:HIS211
|
4.2
|
15.5
|
1.0
|
CG
|
A:HIS205
|
4.3
|
5.5
|
1.0
|
ND1
|
A:HIS205
|
4.3
|
5.3
|
1.0
|
ND1
|
A:HIS201
|
4.3
|
7.3
|
1.0
|
O
|
A:HOH15
|
4.6
|
23.2
|
1.0
|
CE
|
A:MET219
|
4.8
|
3.5
|
1.0
|
OE2
|
A:GLU202
|
4.9
|
12.6
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1cqr
Go back to
Zinc Binding Sites List in 1cqr
Zinc binding site 2 out
of 4 in the Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1302
b:12.4
occ:1.00
|
OD2
|
A:ASP153
|
2.1
|
14.5
|
1.0
|
NE2
|
A:HIS151
|
2.1
|
6.1
|
1.0
|
ND1
|
A:HIS179
|
2.1
|
9.6
|
1.0
|
NE2
|
A:HIS166
|
2.1
|
9.8
|
1.0
|
CD2
|
A:HIS151
|
2.9
|
6.6
|
1.0
|
CE1
|
A:HIS166
|
3.0
|
8.3
|
1.0
|
CG
|
A:ASP153
|
3.0
|
13.9
|
1.0
|
CE1
|
A:HIS179
|
3.0
|
9.1
|
1.0
|
CE1
|
A:HIS151
|
3.1
|
5.6
|
1.0
|
CG
|
A:HIS179
|
3.1
|
8.2
|
1.0
|
CD2
|
A:HIS166
|
3.1
|
8.8
|
1.0
|
OD1
|
A:ASP153
|
3.2
|
11.3
|
1.0
|
CB
|
A:HIS179
|
3.5
|
6.5
|
1.0
|
CG
|
A:HIS151
|
4.1
|
7.1
|
1.0
|
ND1
|
A:HIS166
|
4.1
|
8.5
|
1.0
|
NE2
|
A:HIS179
|
4.1
|
10.6
|
1.0
|
ND1
|
A:HIS151
|
4.1
|
8.0
|
1.0
|
CG
|
A:HIS166
|
4.2
|
7.6
|
1.0
|
CD2
|
A:HIS179
|
4.3
|
8.7
|
1.0
|
O
|
A:TYR155
|
4.3
|
15.9
|
1.0
|
CB
|
A:ASP153
|
4.4
|
12.2
|
1.0
|
OH
|
A:TYR168
|
4.4
|
12.0
|
1.0
|
CZ
|
A:PHE157
|
4.5
|
7.3
|
1.0
|
CE1
|
A:TYR168
|
4.6
|
7.1
|
1.0
|
CE1
|
A:PHE157
|
4.7
|
5.1
|
1.0
|
CA
|
A:HIS179
|
4.9
|
7.4
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1cqr
Go back to
Zinc Binding Sites List in 1cqr
Zinc binding site 3 out
of 4 in the Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn2301
b:21.4
occ:1.00
|
O
|
B:HOH61
|
2.0
|
23.6
|
1.0
|
NE2
|
B:HIS201
|
2.2
|
15.0
|
1.0
|
NE2
|
B:HIS205
|
2.2
|
15.6
|
1.0
|
NE2
|
B:HIS211
|
2.2
|
23.8
|
1.0
|
CD2
|
B:HIS201
|
2.9
|
15.3
|
1.0
|
CD2
|
B:HIS205
|
3.0
|
14.3
|
1.0
|
CE1
|
B:HIS211
|
3.1
|
22.9
|
1.0
|
CD2
|
B:HIS211
|
3.1
|
24.8
|
1.0
|
CE1
|
B:HIS201
|
3.2
|
13.6
|
1.0
|
CE1
|
B:HIS205
|
3.2
|
13.0
|
1.0
|
O
|
B:HOH69
|
3.7
|
23.9
|
1.0
|
OE2
|
B:GLU202
|
4.1
|
14.9
|
1.0
|
CG
|
B:HIS201
|
4.1
|
14.5
|
1.0
|
O
|
B:HOH50
|
4.1
|
17.9
|
1.0
|
ND1
|
B:HIS211
|
4.2
|
25.6
|
1.0
|
CG
|
B:HIS205
|
4.2
|
11.0
|
1.0
|
CG
|
B:HIS211
|
4.2
|
21.6
|
1.0
|
ND1
|
B:HIS201
|
4.2
|
15.4
|
1.0
|
ND1
|
B:HIS205
|
4.3
|
9.3
|
1.0
|
O
|
B:HOH79
|
4.3
|
33.4
|
1.0
|
OE1
|
B:GLU202
|
4.3
|
12.2
|
1.0
|
CD
|
B:GLU202
|
4.6
|
11.9
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1cqr
Go back to
Zinc Binding Sites List in 1cqr
Zinc binding site 4 out
of 4 in the Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn2302
b:15.9
occ:1.00
|
OD2
|
B:ASP153
|
2.0
|
15.7
|
1.0
|
NE2
|
B:HIS166
|
2.1
|
8.0
|
1.0
|
ND1
|
B:HIS179
|
2.1
|
11.6
|
1.0
|
NE2
|
B:HIS151
|
2.1
|
7.7
|
1.0
|
CG
|
B:ASP153
|
2.9
|
11.6
|
1.0
|
CE1
|
B:HIS166
|
2.9
|
8.4
|
1.0
|
CE1
|
B:HIS179
|
2.9
|
8.8
|
1.0
|
CD2
|
B:HIS151
|
3.0
|
5.2
|
1.0
|
OD1
|
B:ASP153
|
3.0
|
13.7
|
1.0
|
CE1
|
B:HIS151
|
3.1
|
9.0
|
1.0
|
CD2
|
B:HIS166
|
3.1
|
10.3
|
1.0
|
CG
|
B:HIS179
|
3.2
|
7.7
|
1.0
|
CB
|
B:HIS179
|
3.6
|
9.5
|
1.0
|
OH
|
B:TYR168
|
3.9
|
14.1
|
1.0
|
ND1
|
B:HIS166
|
4.1
|
10.4
|
1.0
|
NE2
|
B:HIS179
|
4.1
|
10.6
|
1.0
|
CG
|
B:HIS151
|
4.2
|
9.0
|
1.0
|
CG
|
B:HIS166
|
4.2
|
8.8
|
1.0
|
CB
|
B:ASP153
|
4.2
|
10.6
|
1.0
|
O
|
B:TYR155
|
4.2
|
16.3
|
1.0
|
ND1
|
B:HIS151
|
4.2
|
8.7
|
1.0
|
CD2
|
B:HIS179
|
4.3
|
9.8
|
1.0
|
CE1
|
B:TYR168
|
4.5
|
16.1
|
1.0
|
CZ
|
B:PHE157
|
4.6
|
9.7
|
1.0
|
CE1
|
B:PHE157
|
4.6
|
9.1
|
1.0
|
CZ
|
B:TYR168
|
4.7
|
16.4
|
1.0
|
O
|
B:HOH22
|
5.0
|
10.8
|
1.0
|
|
Reference:
L.Chen,
T.J.Rydel,
F.Gu,
C.M.Dunaway,
S.Pikul,
K.M.Dunham,
B.L.Barnett.
Crystal Structure of the Stromelysin Catalytic Domain at 2.0 A Resolution: Inhibitor-Induced Conformational Changes. J.Mol.Biol. V. 293 545 1999.
ISSN: ISSN 0022-2836
PubMed: 10543949
DOI: 10.1006/JMBI.1999.3147
Page generated: Sat Oct 12 23:16:03 2024
|