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Atomistry » Zinc » PDB 1kzo-1lfw » 1lap | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1kzo-1lfw » 1lap » |
Zinc in PDB 1lap: Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms ResolutionEnzymatic activity of Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution
All present enzymatic activity of Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution:
3.4.11.1; Protein crystallography data
The structure of Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution, PDB code: 1lap
was solved by
S.K.Burley,
P.R.David,
A.Taylor,
W.N.Lipscomb,
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 Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution
(pdb code 1lap). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution, PDB code: 1lap: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1lapGo back to Zinc Binding Sites List in 1lap
Zinc binding site 1 out
of 2 in the Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1lapGo back to Zinc Binding Sites List in 1lap
Zinc binding site 2 out
of 2 in the Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution
Mono view Stereo pair view
Reference:
S.K.Burley,
P.R.David,
A.Taylor,
W.N.Lipscomb.
Molecular Structure of Leucine Aminopeptidase at 2.7-A Resolution. Proc.Natl.Acad.Sci.Usa V. 87 6878 1990.
Page generated: Wed Dec 16 02:56:04 2020
ISSN: ISSN 0027-8424 PubMed: 2395881 DOI: 10.1073/PNAS.87.17.6878 |
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