Zinc in PDB 4g09: The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis in Complex with A Substituted Benzyl Ketone

All present enzymatic activity of The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis in Complex with A Substituted Benzyl Ketone:
1.1.1.23;

The structure of The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis in Complex with A Substituted Benzyl Ketone, PDB code: 4g09 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 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	76.654, 105.072, 111.250, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 25.3

The binding sites of Zinc atom in the The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis in Complex with A Substituted Benzyl Ketone (pdb code 4g09). 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 in Complex with A Substituted Benzyl Ketone, PDB code: 4g09:
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 in Complex with A Substituted Benzyl Ketone


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 in Complex with A Substituted Benzyl Ketone within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:33.2 occ:0.70 O A:DMS504 2.1 42.8 0.7 OD2 A:ASP361 2.1 37.9 1.0 NE2 A:HIS262 2.2 40.9 1.0 N3 A:0VD505 2.2 38.2 0.7 N2 A:0VD505 2.2 34.1 0.7 C5 A:0VD505 2.9 40.8 0.7 CD2 A:HIS262 3.1 43.3 1.0 S A:DMS504 3.1 48.4 0.7 C3 A:0VD505 3.1 35.7 0.7 CG A:ASP361 3.1 39.8 1.0 C2 A:0VD505 3.2 33.6 0.7 CE1 A:HIS262 3.2 42.2 1.0 C2 A:DMS504 3.3 44.7 0.7 C4 A:0VD505 3.4 37.7 0.7 OD1 A:ASP361 3.8 39.5 1.0 CB A:ASP361 4.1 36.3 1.0 C1 A:0VD505 4.2 34.6 0.7 CG A:HIS262 4.2 42.1 1.0 N1 A:0VD505 4.2 32.6 0.7 ND1 A:HIS262 4.3 42.4 1.0 C6 A:0VD505 4.3 44.7 0.7 C1 A:DMS504 4.6 44.7 0.7 OE2 A:GLU357 4.6 56.9 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of the C366S Mutant of Hdh From Brucella Suis in Complex with A Substituted Benzyl Ketone


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 in Complex with A Substituted Benzyl Ketone within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:45.3 occ:1.00 OD2 A:ASP313 2.1 37.7 1.0 OD2 A:ASP316 2.3 29.0 1.0 OD1 A:ASP316 2.7 33.5 1.0 OD1 A:ASP313 2.7 35.9 1.0 CG A:ASP316 2.7 32.2 1.0 CG A:ASP313 2.7 36.9 1.0 CB A:ASP316 4.1 27.4 1.0 CB A:ASP313 4.2 35.0 1.0 N A:ASP316 4.3 27.3 1.0 N A:ASP313 4.6 34.5 1.0 CB A:GLU315 4.6 33.6 1.0 CA A:ASP316 4.6 28.5 1.0 CB A:LYS312 4.6 40.0 1.0 CA A:ASP313 4.9 34.5 1.0 O A:ASP313 4.9 32.4 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