Zinc in PDB 4fyw: E. Coli Aspartate Transcarbamoylase Complexed with Ctp

All present enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with Ctp:
2.1.3.2;

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, PDB code: 4fyw was solved by G.M.Cockrell, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.22 / 2.10
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.297, 121.297, 142.251, 90.00, 90.00, 120.00
R / Rfree (%)	18.4 / 22.9

The binding sites of Zinc atom in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp (pdb code 4fyw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, PDB code: 4fyw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Aspartate Transcarbamoylase Complexed with Ctp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:17.7 occ:1.00 SG B:CYS141 2.3 13.7 1.0 SG B:CYS114 2.3 13.8 1.0 SG B:CYS109 2.4 15.0 1.0 SG B:CYS138 2.4 14.3 1.0 CB B:CYS138 3.1 11.5 1.0 CB B:CYS114 3.1 10.5 1.0 CB B:CYS109 3.2 12.4 1.0 CB B:CYS141 3.3 10.6 1.0 N B:CYS141 3.7 11.3 1.0 CA B:CYS141 4.1 18.5 1.0 CA B:CYS114 4.4 16.6 1.0 OG B:SER116 4.4 14.4 1.0 CA B:CYS138 4.6 12.6 1.0 CB B:ASN111 4.6 19.2 1.0 CA B:CYS109 4.7 15.2 1.0 CB B:TYR140 4.7 13.9 1.0 ND2 B:ASN111 4.7 20.9 1.0 C B:TYR140 4.9 10.0 1.0 O B:HOH306 4.9 12.2 1.0 C B:CYS141 5.0 15.3 1.0

Zinc binding site 2 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Aspartate Transcarbamoylase Complexed with Ctp within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:18.6 occ:1.00 SG D:CYS138 2.3 12.8 1.0 SG D:CYS114 2.4 12.8 1.0 SG D:CYS109 2.4 13.3 1.0 SG D:CYS141 2.5 16.5 1.0 CB D:CYS138 3.1 11.0 1.0 CB D:CYS114 3.2 11.8 1.0 CB D:CYS109 3.2 12.2 1.0 CB D:CYS141 3.3 16.3 1.0 N D:CYS141 3.6 13.7 1.0 CA D:CYS141 4.0 17.8 1.0 OG D:SER116 4.4 19.1 1.0 CA D:CYS114 4.4 17.1 1.0 CB D:ASN111 4.6 14.3 1.0 CA D:CYS138 4.6 15.9 1.0 CA D:CYS109 4.7 17.0 1.0 C D:TYR140 4.8 18.0 1.0 CB D:TYR140 4.8 14.0 1.0 ND2 D:ASN111 4.8 17.9 1.0 C D:CYS141 4.9 13.0 1.0 O D:HOH304 5.0 15.0 1.0

G.M.Cockrell, E.R.Kantrowitz. Metal Ion Involvement in the Allosteric Mechanism of Escherichia Coli Aspartate Transcarbamoylase. Biochemistry V. 51 7128 2012.
ISSN: ISSN 0006-2960
PubMed: 22906065
DOI: 10.1021/BI300920M