Atomistry » Zinc » PDB 1z3j-1zfk » 1za2
Atomistry »
  Zinc »
    PDB 1z3j-1zfk »
      1za2 »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy