Zinc in PDB 1ezz: Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State

All present enzymatic activity of Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State:
2.1.3.2;

The structure of Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State, PDB code: 1ezz was solved by L.Jin, B.Stec, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.70
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	129.870, 129.870, 198.340, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 24.2

The binding sites of Zinc atom in the Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State (pdb code 1ezz). 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 E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State, PDB code: 1ezz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State


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 E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn313 b:26.3 occ:1.00 SG B:CYS114 2.3 18.7 1.0 SG B:CYS109 2.3 17.7 1.0 SG B:CYS138 2.4 33.6 1.0 SG B:CYS141 2.4 6.7 1.0 CB B:CYS138 3.2 24.6 1.0 CB B:CYS114 3.3 16.4 1.0 CB B:CYS109 3.3 2.0 1.0 CB B:CYS141 3.4 10.5 1.0 N B:CYS141 3.6 17.8 1.0 CA B:CYS141 4.1 17.6 1.0 OG B:SER116 4.2 12.7 1.0 CB B:TYR140 4.5 5.2 1.0 CB B:ASN111 4.6 17.3 1.0 CA B:CYS114 4.6 19.8 1.0 CA B:CYS109 4.7 11.5 1.0 CA B:CYS138 4.7 25.9 1.0 C B:TYR140 4.8 20.0 1.0 CB B:SER116 4.9 18.9 1.0 ND2 B:ASN111 4.9 33.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State


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 E. Coli Aspartate Transcarbamoylase P268A Mutant in the T-State within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn314 b:20.2 occ:1.00 SG D:CYS141 2.3 11.2 1.0 SG D:CYS114 2.3 10.2 1.0 SG D:CYS138 2.3 17.4 1.0 SG D:CYS109 2.4 26.7 1.0 CB D:CYS114 3.0 16.3 1.0 CB D:CYS109 3.2 30.1 1.0 CB D:CYS138 3.3 17.7 1.0 CB D:CYS141 3.3 2.0 1.0 N D:CYS141 3.6 8.1 1.0 OG D:SER116 3.7 11.5 1.0 CA D:CYS141 4.0 2.0 1.0 ND2 D:ASN111 4.3 2.0 1.0 CB D:ASN111 4.3 10.2 1.0 CA D:CYS114 4.4 10.7 1.0 C D:TYR140 4.6 9.3 1.0 CB D:TYR140 4.6 2.0 1.0 CA D:CYS109 4.7 22.5 1.0 CE2 D:PHE125 4.7 35.8 1.0 CA D:CYS138 4.8 14.7 1.0 N D:TYR140 4.8 13.1 1.0 CG D:ASN111 4.8 2.0 1.0 C D:CYS141 4.9 2.0 1.0 CA D:TYR140 4.9 9.1 1.0 CB D:SER116 4.9 17.1 1.0

L.Jin, B.Stec, E.R.Kantrowitz. A Cis-Proline to Alanine Mutant of E. Coli Aspartate Transcarbamoylase: Kinetic Studies and Three-Dimensional Crystal Structures. Biochemistry V. 39 8058 2000.
ISSN: ISSN 0006-2960
PubMed: 10891088
DOI: 10.1021/BI000418+