Zinc in PDB 9qi5: Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis:
3.5.2.6;

The structure of Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis, PDB code: 9qi5 was solved by A.Chikunova, M.Radojkovic, M.Ubbink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.62 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.161, 40.975, 267.495, 90, 90, 90
R / Rfree (%)	17.4 / 21.1

The binding sites of Zinc atom in the Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis (pdb code 9qi5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis, PDB code: 9qi5:

Zinc binding site 1 out of 1 in the Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of I105R Mutant of Blac From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:73.0 occ:1.00 ND1 B:HIS184 2.2 32.7 1.0 OD1 B:ASP63 2.5 27.4 1.0 OD2 B:ASP63 2.7 32.7 1.0 CG B:ASP63 2.8 30.5 1.0 CE1 B:HIS184 3.0 33.1 1.0 CG B:HIS184 3.2 29.5 1.0 OE1 B:GLU59 3.6 50.0 1.0 CB B:HIS184 3.7 27.5 1.0 CB B:ALA62 4.0 26.2 1.0 NE2 B:HIS184 4.1 32.5 1.0 CE1 B:TYR47 4.2 27.4 1.0 CD2 B:HIS184 4.2 31.3 1.0 CB B:ASP63 4.3 30.1 1.0 O B:HOH443 4.3 37.1 1.0 CD B:GLU59 4.4 49.0 1.0 C B:ALA62 4.5 25.1 1.0 N B:ASP63 4.5 25.2 1.0 CD1 B:TYR47 4.6 27.1 1.0 O B:ALA62 4.7 25.1 1.0 CA B:ASP63 4.8 27.1 1.0 CA B:ALA62 4.8 25.9 1.0 OE2 B:GLU59 4.9 58.1 1.0 CB B:GLU59 4.9 35.7 1.0

M.Radojkovic, S.F.Koene, A.Chikunova, M.Timmer, S.V.Natarajan, M.Ubbink. High-Resolution Activity and Inhibitor Profiling of Residue 105 in Class A Beta-Lactamases To Be Published.