Zinc in PDB 2srt: Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor
Enzymatic activity of Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor
All present enzymatic activity of Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor:
3.4.24.17;
Zinc Binding Sites:
The binding sites of Zinc atom in the Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor
(pdb code 2srt). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor, PDB code: 2srt:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 2srt
Go back to
Zinc Binding Sites List in 2srt
Zinc binding site 1 out
of 2 in the Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn257
b:0.0
occ:1.00
|
O4
|
A:INH256
|
2.1
|
0.0
|
1.0
|
NE2
|
A:HIS201
|
2.1
|
0.0
|
1.0
|
NE2
|
A:HIS211
|
2.2
|
0.0
|
1.0
|
NE2
|
A:HIS205
|
2.2
|
0.0
|
1.0
|
CD2
|
A:HIS211
|
2.7
|
0.0
|
1.0
|
HD2
|
A:HIS211
|
2.8
|
0.0
|
1.0
|
CE1
|
A:HIS201
|
3.0
|
0.0
|
1.0
|
CD2
|
A:HIS201
|
3.1
|
0.0
|
1.0
|
C3
|
A:INH256
|
3.1
|
0.0
|
1.0
|
CE1
|
A:HIS205
|
3.2
|
0.0
|
1.0
|
CD2
|
A:HIS205
|
3.2
|
0.0
|
1.0
|
HE1
|
A:HIS201
|
3.2
|
0.0
|
1.0
|
CE1
|
A:HIS211
|
3.3
|
0.0
|
1.0
|
HE1
|
A:HIS205
|
3.3
|
0.0
|
1.0
|
HD2
|
A:HIS201
|
3.4
|
0.0
|
1.0
|
H70
|
A:INH256
|
3.4
|
0.0
|
1.0
|
HD2
|
A:HIS205
|
3.5
|
0.0
|
1.0
|
H39
|
A:INH256
|
3.7
|
0.0
|
1.0
|
HE1
|
A:HIS211
|
3.8
|
0.0
|
1.0
|
C2
|
A:INH256
|
3.8
|
0.0
|
1.0
|
CG
|
A:HIS211
|
3.9
|
0.0
|
1.0
|
H41
|
A:INH256
|
4.0
|
0.0
|
1.0
|
O5
|
A:INH256
|
4.1
|
0.0
|
1.0
|
N6
|
A:INH256
|
4.1
|
0.0
|
1.0
|
ND1
|
A:HIS211
|
4.2
|
0.0
|
1.0
|
ND1
|
A:HIS201
|
4.2
|
0.0
|
1.0
|
CG
|
A:HIS201
|
4.3
|
0.0
|
1.0
|
ND1
|
A:HIS205
|
4.3
|
0.0
|
1.0
|
CG
|
A:HIS205
|
4.3
|
0.0
|
1.0
|
HE2
|
A:MET219
|
4.4
|
0.0
|
1.0
|
H
|
A:HIS211
|
4.4
|
0.0
|
1.0
|
C7
|
A:INH256
|
4.6
|
0.0
|
1.0
|
O
|
A:MET219
|
4.7
|
0.0
|
1.0
|
H43
|
A:INH256
|
4.8
|
0.0
|
1.0
|
HE3
|
A:MET219
|
4.9
|
0.0
|
1.0
|
HA
|
A:PRO221
|
4.9
|
0.0
|
1.0
|
H40
|
A:INH256
|
5.0
|
0.0
|
1.0
|
N
|
A:HIS211
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 2srt
Go back to
Zinc Binding Sites List in 2srt
Zinc binding site 2 out
of 2 in the Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn258
b:0.0
occ:1.00
|
NE2
|
A:HIS151
|
2.0
|
0.0
|
1.0
|
NE2
|
A:HIS166
|
2.2
|
0.0
|
1.0
|
ND1
|
A:HIS179
|
2.2
|
0.0
|
1.0
|
CE2
|
A:TYR155
|
2.7
|
0.0
|
1.0
|
CE1
|
A:HIS166
|
2.7
|
0.0
|
1.0
|
CZ
|
A:TYR155
|
2.8
|
0.0
|
1.0
|
HE1
|
A:HIS166
|
2.9
|
0.0
|
1.0
|
HE2
|
A:TYR155
|
3.0
|
0.0
|
1.0
|
CD2
|
A:HIS151
|
3.0
|
0.0
|
1.0
|
HB2
|
A:HIS179
|
3.0
|
0.0
|
1.0
|
CE1
|
A:HIS151
|
3.0
|
0.0
|
1.0
|
CD2
|
A:TYR155
|
3.0
|
0.0
|
1.0
|
CD2
|
A:HIS166
|
3.1
|
0.0
|
1.0
|
CE1
|
A:HIS179
|
3.2
|
0.0
|
1.0
|
HD2
|
A:HIS151
|
3.2
|
0.0
|
1.0
|
CG
|
A:HIS179
|
3.3
|
0.0
|
1.0
|
HE1
|
A:HIS151
|
3.3
|
0.0
|
1.0
|
CE1
|
A:TYR155
|
3.3
|
0.0
|
1.0
|
HE1
|
A:HIS179
|
3.3
|
0.0
|
1.0
|
OH
|
A:TYR155
|
3.4
|
0.0
|
1.0
|
CG
|
A:TYR155
|
3.5
|
0.0
|
1.0
|
HE1
|
A:TYR168
|
3.5
|
0.0
|
1.0
|
HD2
|
A:TYR155
|
3.6
|
0.0
|
1.0
|
CB
|
A:HIS179
|
3.6
|
0.0
|
1.0
|
CD1
|
A:TYR155
|
3.6
|
0.0
|
1.0
|
HD2
|
A:HIS166
|
3.6
|
0.0
|
1.0
|
ND1
|
A:HIS166
|
3.7
|
0.0
|
1.0
|
CG
|
A:HIS166
|
4.0
|
0.0
|
1.0
|
HE1
|
A:TYR155
|
4.0
|
0.0
|
1.0
|
HB3
|
A:HIS179
|
4.0
|
0.0
|
1.0
|
HH
|
A:TYR155
|
4.0
|
0.0
|
1.0
|
ND1
|
A:HIS151
|
4.1
|
0.0
|
1.0
|
CG
|
A:HIS151
|
4.2
|
0.0
|
1.0
|
HE2
|
A:PHE157
|
4.3
|
0.0
|
1.0
|
NE2
|
A:HIS179
|
4.3
|
0.0
|
1.0
|
CD2
|
A:HIS179
|
4.4
|
0.0
|
1.0
|
HB2
|
A:TYR155
|
4.4
|
0.0
|
1.0
|
HD1
|
A:TYR155
|
4.4
|
0.0
|
1.0
|
HD1
|
A:HIS166
|
4.5
|
0.0
|
1.0
|
CE1
|
A:TYR168
|
4.5
|
0.0
|
1.0
|
CB
|
A:TYR155
|
4.6
|
0.0
|
1.0
|
HD12
|
A:ILE174
|
4.7
|
0.0
|
1.0
|
H
|
A:HIS179
|
4.8
|
0.0
|
1.0
|
O
|
A:TYR155
|
4.9
|
0.0
|
1.0
|
CA
|
A:HIS179
|
5.0
|
0.0
|
1.0
|
HD2
|
A:PHE157
|
5.0
|
0.0
|
1.0
|
|
Reference:
P.R.Gooley,
J.F.O'connell,
A.I.Marcy,
G.C.Cuca,
S.P.Salowe,
B.L.Bush,
J.D.Hermes,
C.K.Esser,
W.K.Hagmann,
J.P.Springer,
B.A.Johnson.
The uc(Nmr) Structure of the Inhibited Catalytic Domain of Human Stromelysin-1. Nat.Struct.Biol. V. 1 111 1994.
ISSN: ISSN 1072-8368
PubMed: 7656014
DOI: 10.1038/NSB0294-111
Page generated: Thu Oct 17 03:56:16 2024
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