Zinc in PDB 7bz1: The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination.

All present enzymatic activity of The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination.:
3.5.2.6;

The structure of The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination., PDB code: 7bz1 was solved by Y.S.Park, L.W.Kang, J.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.08 / 2.45
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.638, 82.545, 163.716, 90, 110.77, 90
R / Rfree (%)	18.6 / 26

The binding sites of Zinc atom in the The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination. (pdb code 7bz1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination., PDB code: 7bz1:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:22.4 occ:1.00 ND1 A:HIS93 2.1 15.4 1.0 NE2 A:HIS188 2.1 23.6 1.0 NE2 A:HIS91 2.2 8.3 1.0 OD2 A:ASP210 2.3 20.1 1.0 CE1 A:HIS93 2.9 15.7 1.0 CD2 A:HIS91 3.0 8.8 1.0 CE1 A:HIS188 3.1 23.2 1.0 CD2 A:HIS188 3.1 21.8 1.0 CG A:HIS93 3.2 14.8 1.0 CE1 A:HIS91 3.2 8.5 1.0 CG A:ASP210 3.3 20.5 1.0 CB A:HIS93 3.6 16.5 1.0 CB A:ASP210 3.6 19.8 1.0 O A:HOH502 3.9 21.0 1.0 OD1 A:ASP95 3.9 22.1 1.0 NE2 A:HIS93 4.1 14.8 1.0 ND1 A:HIS188 4.2 21.2 1.0 CG A:HIS91 4.2 9.0 1.0 CD2 A:HIS93 4.2 15.5 1.0 CG A:HIS188 4.3 21.5 1.0 ND1 A:HIS91 4.3 9.0 1.0 OD1 A:ASP210 4.3 24.0 1.0 CG A:ASP95 4.8 19.2 1.0 OD2 A:ASP95 4.9 23.0 1.0

Zinc binding site 2 out of 4 in the The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:26.7 occ:1.00 ND1 B:HIS93 2.2 23.0 1.0 NE2 B:HIS91 2.2 15.6 1.0 NE2 B:HIS188 2.2 26.4 1.0 OD2 B:ASP210 2.2 33.9 1.0 O B:HOH501 2.8 26.7 1.0 CD2 B:HIS91 3.0 16.4 1.0 CE1 B:HIS93 3.1 21.9 1.0 CE1 B:HIS188 3.1 25.7 1.0 CG B:HIS93 3.1 21.4 1.0 CG B:ASP210 3.2 33.1 1.0 CD2 B:HIS188 3.3 24.6 1.0 CE1 B:HIS91 3.4 15.2 1.0 CB B:HIS93 3.5 21.0 1.0 OD1 B:ASP95 3.5 35.4 1.0 CB B:ASP210 3.8 30.6 1.0 NE2 B:HIS93 4.2 21.2 1.0 OD1 B:ASP210 4.2 39.0 1.0 CG B:HIS91 4.2 15.6 1.0 CD2 B:HIS93 4.2 19.4 1.0 ND1 B:HIS188 4.2 23.4 1.0 CG B:HIS188 4.3 22.0 1.0 ND1 B:HIS91 4.4 15.4 1.0 CG B:ASP95 4.6 31.9 1.0 NE2 B:HIS279 4.8 43.8 1.0 OD2 B:ASP95 4.9 31.4 1.0 CA B:HIS93 4.9 20.7 1.0 CE1 B:HIS279 5.0 42.6 1.0

Zinc binding site 3 out of 4 in the The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn401 b:30.6 occ:1.00 ND1 C:HIS93 1.8 23.1 1.0 NE2 C:HIS188 2.0 25.6 1.0 NE2 C:HIS91 2.2 18.4 1.0 OD2 C:ASP210 2.6 41.9 1.0 CE1 C:HIS93 2.6 22.5 1.0 CE1 C:HIS188 3.0 25.8 1.0 CD2 C:HIS91 3.0 20.5 1.0 CD2 C:HIS188 3.0 23.2 1.0 CG C:HIS93 3.0 21.5 1.0 CE1 C:HIS91 3.3 20.6 1.0 CG C:ASP210 3.5 38.6 1.0 CB C:HIS93 3.6 21.9 1.0 O C:HOH514 3.6 24.6 1.0 CB C:ASP210 3.8 33.3 1.0 NE2 C:HIS93 3.8 21.6 1.0 OD1 C:ASP95 4.0 36.8 1.0 CD2 C:HIS93 4.0 21.3 1.0 ND1 C:HIS188 4.1 22.7 1.0 CG C:HIS188 4.1 22.9 1.0 CG C:HIS91 4.2 19.7 1.0 ND1 C:HIS91 4.4 18.5 1.0 OD1 C:ASP210 4.4 47.0 1.0 CG C:ASP95 4.9 27.8 1.0 NE2 C:HIS279 4.9 48.9 1.0 OD2 C:ASP95 4.9 30.9 1.0

Zinc binding site 4 out of 4 in the The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Mutant Variant of Pngm-1. H96 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn401 b:24.6 occ:1.00 ND1 D:HIS93 2.0 21.0 1.0 NE2 D:HIS91 2.1 12.9 1.0 NE2 D:HIS188 2.2 29.7 1.0 OD2 D:ASP210 2.2 25.1 1.0 O D:HOH501 2.7 19.7 1.0 CE1 D:HIS93 2.8 20.7 1.0 CE1 D:HIS188 3.0 30.5 1.0 CD2 D:HIS91 3.1 15.3 1.0 CG D:HIS93 3.1 21.3 1.0 CE1 D:HIS91 3.1 14.1 1.0 CG D:ASP210 3.2 24.7 1.0 CD2 D:HIS188 3.3 28.7 1.0 OD1 D:ASP95 3.5 30.2 1.0 CB D:HIS93 3.6 20.7 1.0 CB D:ASP210 3.8 24.3 1.0 NE2 D:HIS93 4.0 21.3 1.0 OD1 D:ASP210 4.0 30.5 1.0 CD2 D:HIS93 4.1 20.4 1.0 ND1 D:HIS188 4.2 28.0 1.0 CG D:HIS91 4.2 15.3 1.0 ND1 D:HIS91 4.2 14.3 1.0 CG D:HIS188 4.3 28.0 1.0 CG D:ASP95 4.5 29.2 1.0 OD2 D:ASP95 4.7 31.1 1.0 NE2 D:HIS279 4.9 40.2 1.0

Y.S.Park, L.W.Kang, J.H.Lee. Structural Study of Metal Binding and Coordination of Ancient Metallo Beta Lactamase Pngm 1 Variants To Be Published.