Zinc in PDB 4if2: Structure of the Phosphotriesterase From Mycobacterium Tuberculosis

The structure of Structure of the Phosphotriesterase From Mycobacterium Tuberculosis, PDB code: 4if2 was solved by L.Zhang, X.Li, Z.H.Rao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.36 / 2.27
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	68.032, 149.596, 74.230, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 22.7

The binding sites of Zinc atom in the Structure of the Phosphotriesterase From Mycobacterium Tuberculosis (pdb code 4if2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Phosphotriesterase From Mycobacterium Tuberculosis, PDB code: 4if2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Phosphotriesterase 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 Structure of the Phosphotriesterase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:29.0 occ:1.00 NE2 A:HIS24 2.0 20.4 1.0 OQ2 A:KCX145 2.1 24.5 1.0 OD1 A:ASP264 2.2 25.4 1.0 CE1 A:HIS22 2.2 18.7 1.0 CG A:ASP264 2.9 23.1 1.0 CE1 A:HIS24 3.0 21.9 1.0 OD2 A:ASP264 3.0 26.1 1.0 CX A:KCX145 3.1 25.2 1.0 NE2 A:HIS22 3.1 27.1 1.0 CD2 A:HIS24 3.1 19.4 1.0 ND1 A:HIS22 3.3 27.0 1.0 ZN A:ZN402 3.3 36.9 1.0 OQ1 A:KCX145 3.5 30.7 1.0 NZ A:KCX145 4.1 24.7 1.0 ND1 A:HIS24 4.1 20.4 1.0 CG A:HIS24 4.2 23.5 1.0 CB A:ASP264 4.3 27.2 1.0 CD2 A:HIS22 4.3 24.8 1.0 O A:HOH508 4.3 33.1 1.0 CE1 A:HIS207 4.4 28.6 1.0 CG A:HIS22 4.4 29.7 1.0 O A:HOH573 4.4 42.1 1.0 NE2 A:HIS207 4.5 27.6 1.0 CA A:ASP264 4.7 25.0 1.0 O A:ASP264 5.0 30.4 1.0

Zinc binding site 2 out of 2 in the Structure of the Phosphotriesterase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Phosphotriesterase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:36.9 occ:1.00 OQ1 A:KCX145 2.2 30.7 1.0 ND1 A:HIS178 2.2 30.5 1.0 NE2 A:HIS207 2.3 27.6 1.0 O A:HOH508 2.6 33.1 1.0 CE1 A:HIS178 3.1 31.3 1.0 CX A:KCX145 3.1 25.2 1.0 OQ2 A:KCX145 3.2 24.5 1.0 CE1 A:HIS207 3.2 28.6 1.0 CD2 A:HIS207 3.3 26.9 1.0 ZN A:ZN401 3.3 29.0 1.0 CG A:HIS178 3.3 25.8 1.0 NH1 A:ARG231 3.4 35.3 1.0 OD2 A:ASP264 3.7 26.1 1.0 CB A:HIS178 3.7 32.0 1.0 NE2 A:HIS22 4.1 27.1 1.0 CZ A:ARG231 4.2 36.9 1.0 CE2 A:TYR98 4.2 28.8 1.0 OH A:TYR98 4.2 39.1 1.0 NE2 A:HIS178 4.3 29.0 1.0 CE1 A:HIS22 4.3 18.7 1.0 ND1 A:HIS207 4.3 33.9 1.0 NZ A:KCX145 4.3 24.7 1.0 CD2 A:HIS178 4.4 28.1 1.0 CG A:HIS207 4.4 30.6 1.0 CA A:HIS178 4.4 25.3 1.0 NE A:ARG231 4.6 28.0 1.0 CG A:ASP264 4.6 23.1 1.0 CZ A:TYR98 4.7 33.5 1.0 OD1 A:ASP264 4.8 25.4 1.0 CE A:KCX145 4.8 28.2 1.0

L.Zhang, X.Li, Z.H.Rao. Crystallization and Structure of the Phosphotriesterase From Mycobacterium Tuberculosis To Be Published.