Zinc in PDB 4g07: The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis

All present enzymatic activity of The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis:
1.1.1.23;

The structure of The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis, PDB code: 4g07 was solved by K.D'ambrosio, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.95
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	76.672, 105.075, 112.416, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 23.9

The binding sites of Zinc atom in the The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis (pdb code 4g07). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis, PDB code: 4g07:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:35.6 occ:0.50 OD2 A:ASP361 2.0 36.5 1.0 OE2 A:GLU357 2.1 52.6 1.0 O A:HOH807 2.1 48.3 1.0 CG A:ASP361 3.0 37.0 1.0 CD A:GLU357 3.1 50.5 1.0 OD1 A:ASP361 3.4 39.3 1.0 CG A:GLU357 4.0 46.7 1.0 OE1 A:GLU357 4.0 53.8 1.0 CB A:ASP361 4.3 34.7 1.0 CA A:VAL358 4.5 30.4 1.0 CG2 A:VAL358 4.7 34.2 1.0 CE1 A:HIS328 4.7 31.4 1.0 N A:VAL358 4.8 31.6 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:27.7 occ:1.00 OD2 A:ASP313 2.0 26.8 1.0 OD2 A:ASP316 2.1 24.6 1.0 CG A:ASP313 2.7 25.1 1.0 CG A:ASP316 2.7 25.0 1.0 OD1 A:ASP313 2.8 20.6 1.0 OD1 A:ASP316 2.8 26.5 1.0 CB A:ASP313 4.2 24.4 1.0 CB A:ASP316 4.2 20.0 1.0 N A:ASP316 4.3 19.4 1.0 N A:ASP313 4.6 22.9 1.0 CB A:GLU315 4.6 25.9 1.0 CA A:ASP316 4.7 20.4 1.0 CB A:LYS312 4.9 30.1 1.0 CA A:ASP313 4.9 24.0 1.0 O A:ASP313 5.0 22.8 1.0

K.D'ambrosio, M.Lopez, N.A.Dathan, S.Ouahrani-Bettache, S.Kohler, G.Ascione, S.M.Monti, J.Y.Winum, G.De Simone. Structural Basis For the Rational Design of New Anti-Brucella Agents: the Crystal Structure of the C366S Mutant of L-Histidinol Dehydrogenase From Brucella Suis. Biochimie V. 97 114 2014.
ISSN: ISSN 0300-9084
PubMed: 24140957
DOI: 10.1016/J.BIOCHI.2013.09.028