Zinc in PDB 4fyv: Aspartate Transcarbamoylase Complexed with Dctp

All present enzymatic activity of Aspartate Transcarbamoylase Complexed with Dctp:
2.1.3.2;

The structure of Aspartate Transcarbamoylase Complexed with Dctp, PDB code: 4fyv 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)	49.06 / 2.10
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.680, 120.680, 142.523, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 21.5

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

Zinc binding site 1 out of 2 in the Aspartate Transcarbamoylase Complexed with Dctp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamoylase Complexed with Dctp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:34.7 occ:1.00 SG B:CYS141 2.3 34.6 1.0 SG B:CYS114 2.3 30.5 1.0 SG B:CYS109 2.4 35.6 1.0 SG B:CYS138 2.4 40.1 1.0 CB B:CYS138 3.0 30.9 1.0 CB B:CYS114 3.1 24.3 1.0 CB B:CYS109 3.2 32.4 1.0 CB B:CYS141 3.3 30.7 1.0 N B:CYS141 3.7 40.0 1.0 CA B:CYS141 4.1 39.8 1.0 CA B:CYS114 4.4 35.4 1.0 CB B:ASN111 4.5 29.8 1.0 ND2 B:ASN111 4.5 33.1 1.0 CA B:CYS138 4.5 45.3 1.0 OG B:SER116 4.5 34.0 1.0 CA B:CYS109 4.6 34.4 1.0 CB B:TYR140 4.7 40.6 1.0 O B:HOH303 4.8 36.5 1.0 C B:TYR140 4.8 37.3 1.0 C B:CYS141 5.0 34.5 1.0

Zinc binding site 2 out of 2 in the Aspartate Transcarbamoylase Complexed with Dctp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamoylase Complexed with Dctp within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:31.0 occ:1.00 SG D:CYS114 2.3 27.9 1.0 SG D:CYS138 2.3 31.4 1.0 SG D:CYS109 2.3 32.7 1.0 SG D:CYS141 2.4 29.8 1.0 CB D:CYS138 3.1 32.8 1.0 CB D:CYS114 3.2 34.2 1.0 CB D:CYS109 3.2 28.8 1.0 CB D:CYS141 3.3 29.3 1.0 N D:CYS141 3.7 30.6 1.0 CA D:CYS141 4.1 31.4 1.0 OG D:SER116 4.4 32.8 1.0 CA D:CYS114 4.4 31.7 1.0 CB D:ASN111 4.5 28.0 1.0 CA D:CYS138 4.6 35.9 1.0 CA D:CYS109 4.6 28.5 1.0 ND2 D:ASN111 4.7 32.7 1.0 CB D:TYR140 4.7 27.2 1.0 O D:HOH304 4.8 34.0 1.0 C D:TYR140 4.8 31.1 1.0 C D:CYS141 5.0 30.1 1.0 N D:TYR140 5.0 25.6 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