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Atomistry » Zinc » PDB 3l2r-3ljg » 3l7r | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3l2r-3ljg » 3l7r » |
Zinc in PDB 3l7r: Crystal Structure of Mete From Streptococcus MutansEnzymatic activity of Crystal Structure of Mete From Streptococcus Mutans
All present enzymatic activity of Crystal Structure of Mete From Streptococcus Mutans:
2.1.1.14; Protein crystallography data
The structure of Crystal Structure of Mete From Streptococcus Mutans, PDB code: 3l7r
was solved by
T.M.Fu,
Y.H.Liang,
X.D.Su,
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 Crystal Structure of Mete From Streptococcus Mutans
(pdb code 3l7r). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Mete From Streptococcus Mutans, PDB code: 3l7r: Jump to Zinc binding site number: 1; 2; 3; Zinc binding site 1 out of 3 in 3l7rGo back to Zinc Binding Sites List in 3l7r
Zinc binding site 1 out
of 3 in the Crystal Structure of Mete From Streptococcus Mutans
Mono view Stereo pair view
Zinc binding site 2 out of 3 in 3l7rGo back to Zinc Binding Sites List in 3l7r
Zinc binding site 2 out
of 3 in the Crystal Structure of Mete From Streptococcus Mutans
Mono view Stereo pair view
Zinc binding site 3 out of 3 in 3l7rGo back to Zinc Binding Sites List in 3l7r
Zinc binding site 3 out
of 3 in the Crystal Structure of Mete From Streptococcus Mutans
Mono view Stereo pair view
Reference:
T.M.Fu,
J.Almqvist,
Y.H.Liang,
L.Li,
Y.Huang,
X.D.Su.
Crystal Structures of Cobalamin-Independent Methionine Synthase (Mete) From Streptococcus Mutans: A Dynamic Zinc-Inversion Model J.Mol.Biol. V. 412 688 2011.
Page generated: Wed Dec 16 04:31:50 2020
ISSN: ISSN 0022-2836 PubMed: 21840320 DOI: 10.1016/J.JMB.2011.08.005 |
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