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Zinc in PDB 6pcz: Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant

Protein crystallography data

The structure of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant, PDB code: 6pcz was solved by A.C.Anderson, T.Brenner, J.T.Weadge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.97 / 1.44
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.710, 94.580, 105.190, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 20.8

Other elements in 6pcz:

The structure of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant (pdb code 6pcz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant, PDB code: 6pcz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6pcz

Go back to Zinc Binding Sites List in 6pcz
Zinc binding site 1 out of 2 in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant


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 the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:20.0
occ:1.00
OE2 A:GLU442 1.9 22.8 1.0
OG A:SER278 1.9 23.0 1.0
NE2 A:HIS443 2.3 20.0 1.0
SG A:CYS243 2.4 24.0 1.0
CB A:SER278 3.0 17.9 1.0
CD A:GLU442 3.1 18.7 1.0
CE1 A:HIS443 3.1 20.0 1.0
CD2 A:HIS443 3.3 18.0 1.0
CB A:CYS243 3.4 18.5 1.0
CA A:SER278 3.6 16.1 1.0
OE1 A:GLU442 3.7 23.6 1.0
CA A:CYS243 3.9 17.9 1.0
N A:SER278 4.0 15.2 1.0
O A:HOH913 4.0 24.5 1.0
CB A:GLU442 4.2 14.3 1.0
ND1 A:HIS443 4.2 15.5 1.0
CG A:GLU442 4.2 17.9 1.0
O A:HOH802 4.3 21.9 1.0
CG A:HIS443 4.3 14.0 1.0
N A:SER244 4.4 18.1 1.0
C A:CYS243 4.7 20.6 1.0
OG A:SER244 4.8 23.3 1.0
C A:TYR277 4.9 16.6 1.0
N A:CYS243 5.0 14.9 1.0
C A:SER278 5.0 15.8 1.0

Zinc binding site 2 out of 2 in 6pcz

Go back to Zinc Binding Sites List in 6pcz
Zinc binding site 2 out of 2 in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:20.0
occ:1.00
OG B:SER278 1.9 23.8 1.0
OE1 B:GLU442 2.1 23.6 1.0
SG B:CYS243 2.3 25.1 1.0
NE2 B:HIS443 2.4 18.5 1.0
CB B:SER278 3.0 18.5 1.0
CE1 B:HIS443 3.0 18.2 1.0
CD B:GLU442 3.3 22.2 1.0
CD2 B:HIS443 3.4 16.6 1.0
CB B:CYS243 3.5 17.7 1.0
CA B:SER278 3.6 15.5 1.0
OE2 B:GLU442 3.9 27.6 1.0
CA B:CYS243 4.0 18.4 1.0
ND1 B:HIS443 4.1 14.3 1.0
CB B:GLU442 4.2 16.7 1.0
N B:SER278 4.2 17.4 1.0
O B:HOH720 4.3 22.8 1.0
CG B:HIS443 4.3 16.1 1.0
CG B:GLU442 4.4 18.1 1.0
N B:SER244 4.5 17.1 1.0
C B:CYS243 4.7 18.3 1.0
OG B:SER244 4.8 19.6 1.0
CD2 B:HIS396 4.8 29.9 1.0
O B:HOH836 4.9 26.1 1.0
C B:SER278 4.9 16.8 1.0
NH1 B:ARG458 5.0 19.8 1.0

Reference:

A.C.Anderson, J.T.Weadge, T.Brenner. Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) Catalytic Domain From Escherichia Coli, Selenomethionine Variant To Be Published.
Page generated: Tue Oct 29 04:57:53 2024

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