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Atomistry » Zinc » PDB 1ed8-1evl » 1ekb » |
Zinc in PDB 1ekb: The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-ChloromethaneEnzymatic activity of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane
All present enzymatic activity of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane:
3.4.21.9; Protein crystallography data
The structure of The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane, PDB code: 1ekb
was solved by
K.Fuetterer,
D.Lu,
J.E.Sadler,
G.Waksman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane
(pdb code 1ekb). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane, PDB code: 1ekb: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1ekbGo back to Zinc Binding Sites List in 1ekb
Zinc binding site 1 out
of 2 in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1ekbGo back to Zinc Binding Sites List in 1ekb
Zinc binding site 2 out
of 2 in the The Serine Protease Domain of Enteropeptidase Bound to Inhibitor Val- Asp-Asp-Asp-Asp-Lys-Chloromethane
Mono view Stereo pair view
Reference:
D.Lu,
K.Futterer,
S.Korolev,
X.Zheng,
K.Tan,
G.Waksman,
J.E.Sadler.
Crystal Structure of Enteropeptidase Light Chain Complexed with An Analog of the Trypsinogen Activation Peptide. J.Mol.Biol. V. 292 361 1999.
Page generated: Sun Oct 13 00:14:01 2024
ISSN: ISSN 0022-2836 PubMed: 10493881 DOI: 10.1006/JMBI.1999.3089 |
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