Zinc in PDB 4fyy: E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+

All present enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+:
2.1.3.2;

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+, PDB code: 4fyy 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)	49.18 / 1.94
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.133, 121.133, 141.438, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 23.7

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+ also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+ (pdb code 4fyy). 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, Utp, and MG2+, PDB code: 4fyy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+


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, Utp, and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:26.0 occ:1.00 SG B:CYS141 2.3 27.9 1.0 SG B:CYS109 2.3 26.6 1.0 SG B:CYS114 2.3 26.8 1.0 SG B:CYS138 2.4 26.7 1.0 CB B:CYS138 3.0 28.4 1.0 CB B:CYS114 3.2 27.4 1.0 CB B:CYS109 3.2 28.9 1.0 CB B:CYS141 3.4 30.2 1.0 N B:CYS141 3.7 27.7 1.0 CA B:CYS141 4.1 29.3 1.0 OG B:SER116 4.4 32.6 1.0 CA B:CYS114 4.5 28.3 1.0 CA B:CYS138 4.5 27.1 1.0 CB B:ASN111 4.5 27.4 1.0 CA B:CYS109 4.6 25.4 1.0 ND2 B:ASN111 4.6 28.7 1.0 CB B:TYR140 4.8 26.4 1.0 C B:TYR140 4.8 30.0 1.0 O B:HOH382 4.9 30.4 1.0

Zinc binding site 2 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+


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, Utp, and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:27.0 occ:1.00 SG D:CYS109 2.3 27.8 1.0 SG D:CYS114 2.4 27.9 1.0 SG D:CYS138 2.4 26.8 1.0 SG D:CYS141 2.5 26.7 1.0 CB D:CYS138 3.1 25.2 1.0 CB D:CYS109 3.2 27.3 1.0 CB D:CYS114 3.2 28.6 1.0 CB D:CYS141 3.3 26.4 1.0 N D:CYS141 3.7 26.9 1.0 CA D:CYS141 4.1 28.9 1.0 OG D:SER116 4.3 30.3 1.0 CA D:CYS114 4.5 29.1 1.0 CB D:ASN111 4.5 28.5 1.0 CA D:CYS138 4.6 30.1 1.0 CA D:CYS109 4.6 25.7 1.0 ND2 D:ASN111 4.7 27.6 1.0 CB D:TYR140 4.7 25.8 1.0 O D:HOH302 4.7 25.8 1.0 C D:TYR140 4.8 26.7 1.0 C D:CYS141 5.0 25.7 1.0 N D:TYR140 5.0 26.9 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