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Atomistry » Zinc » PDB 5cdg-5cup » 5cgz » |
Zinc in PDB 5cgz: Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440Enzymatic activity of Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440
All present enzymatic activity of Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440:
4.2.1.83; Protein crystallography data
The structure of Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440, PDB code: 5cgz
was solved by
S.Mazurkewich,
A.S.Brott,
M.S.Kimber,
S.Y.K.Seah,
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 Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440
(pdb code 5cgz). 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 Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440, PDB code: 5cgz: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5cgzGo back to Zinc Binding Sites List in 5cgz
Zinc binding site 1 out
of 2 in the Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 5cgzGo back to Zinc Binding Sites List in 5cgz
Zinc binding site 2 out
of 2 in the Crystal Structure of Galb, the 4-Carboxy-2-Hydroxymuconate Hydratase, From Pseuodomonas Putida KT2440
Mono view Stereo pair view
Reference:
S.Mazurkewich,
A.S.Brott,
M.S.Kimber,
S.Y.Seah.
Structural and Kinetic Characterization of the 4-Carboxy-2-Hydroxymuconate Hydratase From the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas Putida KT2440. J.Biol.Chem. V. 291 7669 2016.
Page generated: Wed Dec 16 06:06:58 2020
ISSN: ESSN 1083-351X PubMed: 26867578 DOI: 10.1074/JBC.M115.682054 |
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