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Atomistry » Zinc » PDB 5fz6-5g1c » 5g1a | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 5fz6-5g1c » 5g1a » |
Zinc in PDB 5g1a: Bordetella Alcaligenes Hdah Bound to PfsahaEnzymatic activity of Bordetella Alcaligenes Hdah Bound to Pfsaha
All present enzymatic activity of Bordetella Alcaligenes Hdah Bound to Pfsaha:
3.5.1.4; Protein crystallography data
The structure of Bordetella Alcaligenes Hdah Bound to Pfsaha, PDB code: 5g1a
was solved by
A.Kraemer,
F.J.Meyer-Almes,
O.Yildiz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5g1a:
The structure of Bordetella Alcaligenes Hdah Bound to Pfsaha also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Bordetella Alcaligenes Hdah Bound to Pfsaha
(pdb code 5g1a). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Bordetella Alcaligenes Hdah Bound to Pfsaha, PDB code: 5g1a: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5g1aGo back to Zinc Binding Sites List in 5g1a
Zinc binding site 1 out
of 2 in the Bordetella Alcaligenes Hdah Bound to Pfsaha
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 5g1aGo back to Zinc Binding Sites List in 5g1a
Zinc binding site 2 out
of 2 in the Bordetella Alcaligenes Hdah Bound to Pfsaha
Mono view Stereo pair view
Reference:
C.Meyners,
A.Kramer,
O.Yildiz,
F.J.Meyer-Almes.
The Thermodynamic Signature of Ligand Binding to Histone Deacetylase-Like Amidohydrolases Is Most Sensitive to the Flexibility in the L2-Loop Lining the Active Site Pocket. Biochim. Biophys. Acta V.1861 1855 2017.
Page generated: Sun Oct 27 16:52:20 2024
ISSN: ISSN 0006-3002 PubMed: 28389333 DOI: 10.1016/J.BBAGEN.2017.04.001 |
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