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Atomistry » Zinc » PDB 4gsl-4gy0 » 4gwm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4gsl-4gy0 » 4gwm » |
Zinc in PDB 4gwm: Crystal Structure of Human Promeprin BetaEnzymatic activity of Crystal Structure of Human Promeprin Beta
All present enzymatic activity of Crystal Structure of Human Promeprin Beta:
3.4.24.63; Protein crystallography data
The structure of Crystal Structure of Human Promeprin Beta, PDB code: 4gwm
was solved by
J.L.Arolas,
C.Broder,
T.Jefferson,
T.Guevara,
E.E.Sterchi,
W.Bode,
W.Stocker,
C.Becker-Pauly,
F.X.Gomis-Ruth,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4gwm:
The structure of Crystal Structure of Human Promeprin Beta also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human Promeprin Beta
(pdb code 4gwm). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Promeprin Beta, PDB code: 4gwm: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 4gwmGo back to Zinc Binding Sites List in 4gwm
Zinc binding site 1 out
of 2 in the Crystal Structure of Human Promeprin Beta
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 4gwmGo back to Zinc Binding Sites List in 4gwm
Zinc binding site 2 out
of 2 in the Crystal Structure of Human Promeprin Beta
Mono view Stereo pair view
Reference:
J.L.Arolas,
C.Broder,
T.Jefferson,
T.Guevara,
E.E.Sterchi,
W.Bode,
W.Stocker,
C.Becker-Pauly,
F.X.Gomis-Ruth.
Structural Basis For the Sheddase Function of Human Meprin Beta Metalloproteinase at the Plasma Membrane Proc.Natl.Acad.Sci.Usa V. 109 16131 2012.
Page generated: Wed Dec 16 05:21:03 2020
ISSN: ISSN 0027-8424 PubMed: 22988105 DOI: 10.1073/PNAS.1211076109 |
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