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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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