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Atomistry » Zinc » PDB 3kej-3kr5 » 3khi » |
Zinc in PDB 3khi: Crystal Structure of A Putative Metal-Dependent Hydrolase (YP_001336084.1) From Klebsiella Pneumoniae Subsp. Pneumoniae Mgh 78578 at 1.95 A ResolutionProtein crystallography data
The structure of Crystal Structure of A Putative Metal-Dependent Hydrolase (YP_001336084.1) From Klebsiella Pneumoniae Subsp. Pneumoniae Mgh 78578 at 1.95 A Resolution, PDB code: 3khi
was solved by
Joint Center For Structural Genomics (Jcsg),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3khi:
The structure of Crystal Structure of A Putative Metal-Dependent Hydrolase (YP_001336084.1) From Klebsiella Pneumoniae Subsp. Pneumoniae Mgh 78578 at 1.95 A Resolution also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of A Putative Metal-Dependent Hydrolase (YP_001336084.1) From Klebsiella Pneumoniae Subsp. Pneumoniae Mgh 78578 at 1.95 A Resolution
(pdb code 3khi). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of A Putative Metal-Dependent Hydrolase (YP_001336084.1) From Klebsiella Pneumoniae Subsp. Pneumoniae Mgh 78578 at 1.95 A Resolution, PDB code: 3khi: Zinc binding site 1 out of 1 in 3khiGo back to Zinc Binding Sites List in 3khi
Zinc binding site 1 out
of 1 in the Crystal Structure of A Putative Metal-Dependent Hydrolase (YP_001336084.1) From Klebsiella Pneumoniae Subsp. Pneumoniae Mgh 78578 at 1.95 A Resolution
Mono view Stereo pair view
Reference:
Q.Xu,
A.K.Gohler,
A.Kosfeld,
D.Carlton,
H.J.Chiu,
H.E.Klock,
M.W.Knuth,
M.D.Miller,
M.A.Elsliger,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
K.Jahreis,
I.A.Wilson.
The Structure of Mlc Titration Factor A (Mtfa/Yeei) Reveals A Prototypical Zinc Metallopeptidase Related to Anthrax Lethal Factor. J.Bacteriol. V. 194 2987 2012.
Page generated: Wed Dec 16 04:30:12 2020
ISSN: ISSN 0021-9193 PubMed: 22467785 DOI: 10.1128/JB.00038-12 |
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