Zinc in PDB 1xjw: The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State

All present enzymatic activity of The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State:
2.1.3.2;

The structure of The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State, PDB code: 1xjw was solved by K.A.Stieglitz, N.Alam, J.Xia, S.Gourinath, H.Tsuruta, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.71
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.116, 122.116, 155.928, 90.00, 90.00, 120.00
R / Rfree (%)	17 / 22.3

The binding sites of Zinc atom in the The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State (pdb code 1xjw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State, PDB code: 1xjw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1313 b:34.5 occ:1.00 SG B:CYS141 2.3 30.0 1.0 SG B:CYS114 2.3 27.3 1.0 SG B:CYS109 2.3 31.3 1.0 SG B:CYS138 2.3 30.1 1.0 CB B:CYS138 3.1 31.1 1.0 CB B:CYS141 3.2 28.8 1.0 CB B:CYS114 3.2 27.7 1.0 CB B:CYS109 3.2 31.9 1.0 N B:CYS141 3.6 25.8 1.0 CA B:CYS141 4.0 27.4 1.0 OG B:SER116 4.2 27.2 1.0 CA B:CYS114 4.5 26.6 1.0 CA B:CYS138 4.5 32.5 1.0 CB B:ASN111 4.6 28.8 1.0 CB B:TYR140 4.7 24.5 1.0 CA B:CYS109 4.7 33.8 1.0 C B:TYR140 4.8 24.4 1.0 ND2 B:ASN111 4.8 27.5 1.0 C B:CYS141 4.8 27.6 1.0 N B:GLU142 4.9 30.0 1.0

Zinc binding site 2 out of 2 in the The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of E. Coli Aspartate Transcarbamoylase Q137A Mutant in the R-State within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1314 b:32.9 occ:1.00 SG D:CYS138 2.3 27.2 1.0 SG D:CYS114 2.3 26.8 1.0 SG D:CYS141 2.4 26.4 1.0 SG D:CYS109 2.4 27.6 1.0 CB D:CYS138 3.1 28.9 1.0 CB D:CYS114 3.1 26.6 1.0 CB D:CYS109 3.3 27.7 1.0 CB D:CYS141 3.3 28.2 1.0 N D:CYS141 3.6 28.0 1.0 CA D:CYS141 4.0 29.1 1.0 OG D:SER116 4.3 31.6 1.0 CA D:CYS114 4.4 25.8 1.0 ND2 D:ASN111 4.5 32.3 1.0 CB D:TYR140 4.5 27.5 1.0 CA D:CYS138 4.5 31.1 1.0 CB D:ASN111 4.7 31.0 1.0 C D:TYR140 4.7 28.5 1.0 CA D:CYS109 4.7 29.5 1.0 CA D:TYR140 4.9 28.5 1.0 C D:CYS141 4.9 30.1 1.0 N D:TYR140 4.9 30.2 1.0 CB D:SER116 5.0 28.1 1.0

K.A.Stieglitz, S.C.Pastra-Landis, J.Xia, H.Tsuruta, E.R.Kantrowitz. A Single Amino Acid Substitution in the Active Site of Escherichia Coli Aspartate Transcarbamoylase Prevents the Allosteric Transition. J.Mol.Biol. V. 349 413 2005.
ISSN: ISSN 0022-2836
PubMed: 15890205
DOI: 10.1016/J.JMB.2005.03.073