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Atomistry » Magnesium » PDB 4wxw-4x7v » 4x5b » |
Magnesium in PDB 4x5b: Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and MgEnzymatic activity of Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg
All present enzymatic activity of Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg:
2.4.2.18; Protein crystallography data
The structure of Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg, PDB code: 4x5b
was solved by
T.V.M.Cookson,
E.J.Parker,
J.S.Lott,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg
(pdb code 4x5b). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg, PDB code: 4x5b: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 4x5bGo back to Magnesium Binding Sites List in 4x5b
Magnesium binding site 1 out
of 2 in the Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 4x5bGo back to Magnesium Binding Sites List in 4x5b
Magnesium binding site 2 out
of 2 in the Anthranilate Phosphoribosyltransferase Variant R193L From Mycobacterium Tuberculosis in Complex with Prpp and Mg
Mono view Stereo pair view
Reference:
T.V.Cookson,
G.L.Evans,
A.Castell,
E.N.Baker,
J.S.Lott,
E.J.Parker.
Structures of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site. Biochemistry V. 54 6082 2015.
Page generated: Tue Aug 20 14:04:44 2024
ISSN: ISSN 0006-2960 PubMed: 26356348 DOI: 10.1021/ACS.BIOCHEM.5B00612 |
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