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Zinc in PDB 1za2: Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution

Enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution

All present enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution:
2.1.3.2;

Protein crystallography data

The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution, PDB code: 1za2 was solved by J.Wang, K.A.Stieglitz, J.P.Cardia, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.442, 121.442, 142.547, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 25.1

Other elements in 1za2:

The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution (pdb code 1za2). 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 Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution, PDB code: 1za2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1za2

Go back to Zinc Binding Sites List in 1za2
Zinc binding site 1 out of 2 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn154

b:35.2
occ:1.00
SG B:CYS138 2.3 35.3 1.0
SG B:CYS114 2.3 34.3 1.0
SG B:CYS109 2.3 37.0 1.0
SG B:CYS141 2.4 34.1 1.0
CB B:CYS138 3.1 35.0 1.0
CB B:CYS114 3.1 35.5 1.0
CB B:CYS109 3.3 35.8 1.0
CB B:CYS141 3.4 33.9 1.0
N B:CYS141 3.7 33.2 1.0
CA B:CYS141 4.1 34.7 1.0
OG B:SER116 4.3 36.9 1.0
CA B:CYS114 4.5 35.4 1.0
CB B:TYR140 4.5 33.0 1.0
CA B:CYS138 4.6 34.9 1.0
CB B:ASN111 4.6 37.3 1.0
O B:HOH160 4.6 31.1 1.0
CA B:CYS109 4.7 37.1 1.0
ND2 B:ASN111 4.8 41.0 1.0
C B:TYR140 4.8 33.5 1.0
C B:CYS141 5.0 35.7 1.0

Zinc binding site 2 out of 2 in 1za2

Go back to Zinc Binding Sites List in 1za2
Zinc binding site 2 out of 2 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn154

b:37.1
occ:1.00
SG D:CYS114 2.3 35.1 1.0
SG D:CYS109 2.3 35.8 1.0
SG D:CYS141 2.4 39.1 1.0
SG D:CYS138 2.4 35.3 1.0
CB D:CYS141 2.8 40.0 1.0
CB D:CYS114 3.0 36.6 1.0
CB D:CYS138 3.2 39.7 1.0
CB D:CYS109 3.3 37.9 1.0
N D:CYS141 3.7 37.7 1.0
CA D:CYS141 3.7 40.1 1.0
OG D:SER116 4.3 34.5 1.0
CA D:CYS114 4.4 36.3 1.0
CB D:ASN111 4.5 38.0 1.0
ND2 D:ASN111 4.6 32.4 1.0
CA D:CYS109 4.7 38.7 1.0
CA D:CYS138 4.7 40.3 1.0
CB D:TYR140 4.8 36.7 1.0
C D:TYR140 4.8 39.1 1.0
O D:ASN111 4.9 38.4 1.0

Reference:

J.Wang, K.A.Stieglitz, J.P.Cardia, E.R.Kantrowitz. Structural Basis For Ordered Substrate Binding and Cooperativity in Aspartate Transcarbamoylase Proc.Natl.Acad.Sci.Usa V. 102 8881 2005.
ISSN: ISSN 0027-8424
PubMed: 15951418
DOI: 10.1073/PNAS.0503742102
Page generated: Wed Oct 16 21:10:48 2024

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