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Atomistry » Zinc » PDB 5h6b-5ho1 » 5hms » |
Zinc in PDB 5hms: X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad).Enzymatic activity of X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad).
All present enzymatic activity of X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad).:
4.2.1.24; Protein crystallography data
The structure of X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad)., PDB code: 5hms
was solved by
D.Butler,
P.T.Erskine,
J.B.Cooper,
P.M.Shoolingin-Jordan,
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 X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad).
(pdb code 5hms). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad)., PDB code: 5hms: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5hmsGo back to Zinc Binding Sites List in 5hms
Zinc binding site 1 out
of 2 in the X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad).
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 5hmsGo back to Zinc Binding Sites List in 5hms
Zinc binding site 2 out
of 2 in the X-Ray Structure of Human Recombinant 5-Aminolaevulinic Acid Dehydratase (Hralad).
Mono view Stereo pair view
Reference:
N.Mills-Davies,
D.Butler,
E.Norton,
D.Thompson,
M.Sarwar,
J.Guo,
R.Gill,
N.Azim,
A.Coker,
S.P.Wood,
P.T.Erskine,
L.Coates,
J.B.Cooper,
N.Rashid,
M.Akhtar,
P.M.Shoolingin-Jordan.
Structural Studies of Substrate and Product Complexes of 5-Aminolaevulinic Acid Dehydratase From Humans, Escherichia Coli and the Hyperthermophile Pyrobaculum Calidifontis. Acta Crystallogr D Struct V. 73 9 2017BIOL.
Page generated: Sun Oct 27 17:32:56 2024
ISSN: ISSN 2059-7983 PubMed: 28045381 DOI: 10.1107/S2059798316019525 |
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