Zinc in PDB 1za1: Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp at 2.20 A Resolution

All present enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp at 2.20 A Resolution:
2.1.3.2;

The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp at 2.20 A Resolution, PDB code: 1za1 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 / 2.20
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.294, 120.294, 142.555, 90.00, 90.00, 120.00
R / Rfree (%)	20.5 / 25.2

The binding sites of Zinc atom in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp at 2.20 A Resolution (pdb code 1za1). 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 at 2.20 A Resolution, PDB code: 1za1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp at 2.20 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 at 2.20 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:32.3 occ:1.00 SG B:CYS141 2.5 26.6 1.0 SG B:CYS109 2.5 29.4 1.0 SG B:CYS114 2.5 22.6 1.0 SG B:CYS138 2.5 30.4 1.0 CB B:CYS138 3.0 24.8 1.0 CB B:CYS114 3.2 15.6 1.0 CB B:CYS109 3.2 20.8 1.0 CB B:CYS141 3.5 22.2 1.0 N B:CYS141 3.7 19.3 1.0 CA B:CYS141 4.2 35.0 1.0 OG B:SER116 4.4 28.3 1.0 CA B:CYS114 4.5 26.5 1.0 CA B:CYS138 4.5 36.0 1.0 ND2 B:ASN111 4.7 25.2 1.0 CB B:ASN111 4.7 25.9 1.0 CA B:CYS109 4.7 28.1 1.0 CB B:TYR140 4.8 31.5 1.0 C B:TYR140 4.9 25.0 1.0 O B:HOH903 4.9 34.1 1.0 C B:CYS141 5.0 34.3 1.0

Zinc binding site 2 out of 2 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp at 2.20 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 at 2.20 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:29.1 occ:1.00 SG D:CYS114 2.3 20.9 1.0 SG D:CYS138 2.4 23.5 1.0 SG D:CYS109 2.4 23.1 1.0 SG D:CYS141 2.4 25.2 1.0 CB D:CYS138 3.0 15.2 1.0 CB D:CYS114 3.2 16.6 1.0 CB D:CYS109 3.2 21.9 1.0 CB D:CYS141 3.4 26.5 1.0 N D:CYS141 3.7 18.9 1.0 CA D:CYS141 4.2 22.5 1.0 OG D:SER116 4.3 28.3 1.0 CA D:CYS114 4.4 19.7 1.0 CB D:ASN111 4.5 19.5 1.0 CA D:CYS138 4.5 28.1 1.0 O D:HOH905 4.6 26.7 1.0 CA D:CYS109 4.6 28.0 1.0 CB D:TYR140 4.7 28.4 1.0 ND2 D:ASN111 4.7 23.9 1.0 C D:TYR140 4.8 23.0 1.0 C D:CYS141 5.0 25.8 1.0 N D:TYR140 5.0 20.1 1.0

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