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Atomistry » Zinc » PDB 2rv3-2v1c » 2srt | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2rv3-2v1c » 2srt » |
Zinc in PDB 2srt: Catalytic Domain of Human Stromelysin-1 at pH 5.5 and 40OC Complexed with InhibitorEnzymatic 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 2srtGo 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
Zinc binding site 2 out of 2 in 2srtGo 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
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.
Page generated: Thu Oct 17 03:56:16 2024
ISSN: ISSN 1072-8368 PubMed: 7656014 DOI: 10.1038/NSB0294-111 |
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