Zinc in PDB 7bz4: The Mutant Variant of Pngm-1. H279 Was Substituted For Alanine to Study Metal Coordination.

Enzymatic activity of The Mutant Variant of Pngm-1. H279 Was Substituted For Alanine to Study Metal Coordination.

All present enzymatic activity of The Mutant Variant of Pngm-1. H279 Was Substituted For Alanine to Study Metal Coordination.:
3.5.2.6;

Protein crystallography data

The structure of The Mutant Variant of Pngm-1. H279 Was Substituted For Alanine to Study Metal Coordination., PDB code: 7bz4 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 / 2.16
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.857, 82.964, 164.037, 90, 110.94, 90
R / Rfree (%) 19.3 / 24.9

Zinc Binding Sites:

The binding sites of Zinc atom in the The Mutant Variant of Pngm-1. H279 Was Substituted For Alanine to Study Metal Coordination. (pdb code 7bz4). 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. H279 Was Substituted For Alanine to Study Metal Coordination., PDB code: 7bz4:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 7bz4

Go back to Zinc Binding Sites List in 7bz4
Zinc binding site 1 out of 4 in the The Mutant Variant of Pngm-1. H279 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. H279 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:12.0
occ:1.00
O A:HOH559 2.0 16.1 1.0
ND1 A:HIS93 2.0 6.5 1.0
NE2 A:HIS188 2.1 11.5 1.0
O A:HOH608 2.1 20.1 1.0
NE2 A:HIS91 2.2 4.7 1.0
OD2 A:ASP210 2.3 8.7 1.0
CE1 A:HIS93 2.9 6.5 1.0
CE1 A:HIS188 3.0 11.4 1.0
CD2 A:HIS188 3.0 11.2 1.0
CD2 A:HIS91 3.1 4.7 1.0
CG A:HIS93 3.1 6.9 1.0
CG A:ASP210 3.2 9.1 1.0
CE1 A:HIS91 3.3 4.7 1.0
O A:HOH501 3.3 21.7 1.0
CB A:HIS93 3.6 7.1 1.0
CB A:ASP210 3.6 9.4 1.0
O A:HOH690 4.0 37.0 1.0
NE2 A:HIS93 4.1 6.7 1.0
CD2 A:HIS96 4.1 7.8 1.0
ND1 A:HIS188 4.1 10.8 1.0
NE2 A:HIS96 4.1 7.8 1.0
CG A:HIS188 4.2 11.3 1.0
CD2 A:HIS93 4.2 6.5 1.0
CG A:HIS91 4.3 4.6 1.0
ND1 A:HIS91 4.3 4.6 1.0
OD1 A:ASP210 4.3 9.9 1.0
CA A:HIS93 5.0 7.2 1.0

Zinc binding site 2 out of 4 in 7bz4

Go back to Zinc Binding Sites List in 7bz4
Zinc binding site 2 out of 4 in the The Mutant Variant of Pngm-1. H279 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. H279 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:21.1
occ:1.00
O B:HOH505 2.0 16.7 1.0
ND1 B:HIS93 2.1 13.7 1.0
NE2 B:HIS188 2.1 15.0 1.0
NE2 B:HIS91 2.3 10.8 1.0
OD2 B:ASP210 2.4 14.2 1.0
O B:HOH577 2.4 24.6 1.0
CD2 B:HIS188 3.0 15.6 1.0
CE1 B:HIS93 3.0 14.2 1.0
CD2 B:HIS91 3.1 10.4 1.0
CG B:HIS93 3.2 12.8 1.0
CE1 B:HIS188 3.2 15.5 1.0
O B:HOH501 3.3 18.6 1.0
CE1 B:HIS91 3.3 10.6 1.0
CG B:ASP210 3.5 15.2 1.0
CB B:HIS93 3.5 12.8 1.0
CB B:ASP210 3.8 15.2 1.0
NE2 B:HIS96 3.9 11.9 1.0
CD2 B:HIS96 3.9 11.8 1.0
CG B:HIS188 4.1 15.2 1.0
NE2 B:HIS93 4.2 13.5 1.0
ND1 B:HIS188 4.2 14.7 1.0
CD2 B:HIS93 4.2 12.8 1.0
OD1 B:ASP95 4.3 45.3 1.0
CG B:HIS91 4.3 10.1 1.0
ND1 B:HIS91 4.4 9.6 1.0
OD1 B:ASP210 4.6 16.9 1.0
OD2 B:ASP95 4.7 42.9 1.0
CG B:ASP95 4.9 36.1 1.0
CE1 B:HIS96 4.9 12.4 1.0
CG B:HIS96 4.9 11.9 1.0
CA B:HIS93 5.0 13.0 1.0

Zinc binding site 3 out of 4 in 7bz4

Go back to Zinc Binding Sites List in 7bz4
Zinc binding site 3 out of 4 in the The Mutant Variant of Pngm-1. H279 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. H279 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:20.8
occ:1.00
NE2 C:HIS91 2.0 16.0 1.0
NE2 C:HIS188 2.1 18.4 1.0
ND1 C:HIS93 2.2 14.2 1.0
OD2 C:ASP210 2.3 19.0 1.0
O C:HOH547 2.5 25.4 1.0
O C:HOH522 2.5 18.0 1.0
CD2 C:HIS188 2.8 19.4 1.0
O C:HOH503 2.9 40.5 1.0
CD2 C:HIS91 3.0 16.5 1.0
CE1 C:HIS91 3.0 16.9 1.0
CE1 C:HIS93 3.1 14.2 1.0
CG C:HIS93 3.3 13.6 1.0
CE1 C:HIS188 3.3 18.9 1.0
CG C:ASP210 3.3 20.2 1.0
CB C:HIS93 3.7 14.4 1.0
CB C:ASP210 3.7 20.1 1.0
NE2 C:HIS96 3.9 16.6 1.0
CG C:HIS188 4.0 20.9 1.0
CD2 C:HIS96 4.1 17.5 1.0
CG C:HIS91 4.1 16.2 1.0
ND1 C:HIS91 4.1 15.2 1.0
NE2 C:HIS93 4.2 15.3 1.0
ND1 C:HIS188 4.2 18.9 1.0
OD1 C:ASP95 4.3 44.1 1.0
CD2 C:HIS93 4.3 14.4 1.0
OD1 C:ASP210 4.4 21.8 1.0
CE1 C:HIS96 4.8 17.7 1.0

Zinc binding site 4 out of 4 in 7bz4

Go back to Zinc Binding Sites List in 7bz4
Zinc binding site 4 out of 4 in the The Mutant Variant of Pngm-1. H279 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. H279 Was Substituted For Alanine to Study Metal Coordination. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn401

b:15.5
occ:1.00
O D:HOH568 1.8 13.0 1.0
ND1 D:HIS93 2.0 7.5 1.0
NE2 D:HIS91 2.0 7.6 1.0
NE2 D:HIS188 2.2 11.2 1.0
O D:HOH611 2.3 4.5 1.0
OD2 D:ASP210 2.3 14.9 1.0
CE1 D:HIS93 2.9 7.4 1.0
CD2 D:HIS91 3.0 7.7 1.0
CE1 D:HIS188 3.0 10.6 1.0
CE1 D:HIS91 3.1 8.0 1.0
CG D:HIS93 3.1 7.5 1.0
CD2 D:HIS188 3.2 11.0 1.0
O D:HOH503 3.3 18.0 1.0
CG D:ASP210 3.4 14.7 1.0
CB D:HIS93 3.6 7.9 1.0
CB D:ASP210 3.8 13.6 1.0
CD2 D:HIS96 4.0 8.3 1.0
NE2 D:HIS96 4.0 8.2 1.0
NE2 D:HIS93 4.1 7.2 1.0
ND1 D:HIS188 4.1 11.4 1.0
ND1 D:HIS91 4.2 7.6 1.0
CD2 D:HIS93 4.2 7.3 1.0
CG D:HIS91 4.2 7.6 1.0
CG D:HIS188 4.2 11.5 1.0
OD1 D:ASP210 4.5 18.4 1.0
O A:HOH661 4.7 31.8 1.0
CG D:HIS96 4.9 8.3 1.0
CE1 D:HIS96 4.9 8.2 1.0
CA D:HIS93 5.0 8.4 1.0

Reference:

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.
Page generated: Mon Jul 12 16:57:29 2021

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