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Atomistry » Zinc » PDB 3e2d-3eb5 » 3e7f » |
Zinc in PDB 3e7f: Crystal Structure of 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic AcidEnzymatic activity of Crystal Structure of 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid
All present enzymatic activity of Crystal Structure of 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid:
3.1.1.17; Protein crystallography data
The structure of Crystal Structure of 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid, PDB code: 3e7f
was solved by
L.Poggi,
M.Delarue,
N.Duclert-Savatier,
V.Stoven,
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 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid
(pdb code 3e7f). 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 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid, PDB code: 3e7f: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3e7fGo back to Zinc Binding Sites List in 3e7f
Zinc binding site 1 out
of 2 in the Crystal Structure of 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 3e7fGo back to Zinc Binding Sites List in 3e7f
Zinc binding site 2 out
of 2 in the Crystal Structure of 6-Phosphogluconolactonase From Trypanosoma Brucei Complexed with 6-Phosphogluconic Acid
Mono view Stereo pair view
Reference:
N.Duclert-Savatier,
L.Poggi,
E.Miclet,
P.Lopes,
J.Ouazzani,
N.Chevalier,
M.Nilges,
M.Delarue,
V.Stoven.
Insights Into the Enzymatic Mechanism of 6-Phosphogluconolactonase From Trypanosoma Brucei Using Structural Data and Molecular Dynamics Simulation. J.Mol.Biol. V. 388 1009 2009.
Page generated: Thu Oct 24 12:38:52 2024
ISSN: ISSN 0022-2836 PubMed: 19345229 DOI: 10.1016/J.JMB.2009.03.063 |
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