Zinc in PDB 4kgx: The R State Structure of E. Coli Atcase with Ctp Bound

All present enzymatic activity of The R State Structure of E. Coli Atcase with Ctp Bound:
2.1.3.2;

The structure of The R State Structure of E. Coli Atcase with Ctp Bound, PDB code: 4kgx was solved by G.M.Cockrell, Y.Zheng, W.Guo, A.W.Peterson, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.72 / 2.20
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.237, 121.237, 154.772, 90.00, 90.00, 120.00
R / Rfree (%)	15.6 / 19.2

The binding sites of Zinc atom in the The R State Structure of E. Coli Atcase with Ctp Bound (pdb code 4kgx). 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 R State Structure of E. Coli Atcase with Ctp Bound, PDB code: 4kgx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The R State Structure of E. Coli Atcase with Ctp Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The R State Structure of E. Coli Atcase with Ctp Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:25.7 occ:1.00 SG B:CYS141 2.3 27.7 1.0 SG B:CYS138 2.3 22.3 1.0 SG B:CYS109 2.3 26.3 1.0 SG B:CYS114 2.4 25.9 1.0 CB B:CYS138 3.1 19.1 1.0 CB B:CYS114 3.1 26.9 1.0 CB B:CYS109 3.2 18.7 1.0 CB B:CYS141 3.3 27.0 1.0 N B:CYS141 3.7 23.3 1.0 CA B:CYS141 4.1 26.7 1.0 OG B:SER116 4.4 24.7 1.0 CA B:CYS114 4.4 26.7 1.0 CB B:ASN111 4.5 37.0 1.0 CA B:CYS138 4.6 21.1 1.0 CA B:CYS109 4.7 29.9 1.0 ND2 B:ASN111 4.7 23.6 1.0 CB B:TYR140 4.7 24.7 1.0 O B:HOH303 4.8 24.4 1.0 C B:TYR140 4.9 25.1 1.0 C B:CYS141 5.0 24.4 1.0

Zinc binding site 2 out of 2 in the The R State Structure of E. Coli Atcase with Ctp Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The R State Structure of E. Coli Atcase with Ctp Bound within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:35.3 occ:1.00 SG D:CYS141 2.3 36.8 1.0 SG D:CYS114 2.3 34.3 1.0 SG D:CYS138 2.3 32.5 1.0 SG D:CYS109 2.4 33.9 1.0 CB D:CYS138 3.1 25.1 1.0 CB D:CYS109 3.2 22.2 1.0 CB D:CYS114 3.2 36.5 1.0 CB D:CYS141 3.3 33.0 1.0 N D:CYS141 3.7 33.1 1.0 CA D:CYS141 4.1 33.9 1.0 OG D:SER116 4.4 35.3 1.0 CA D:CYS114 4.5 36.6 1.0 CB D:ASN111 4.5 39.6 1.0 CA D:CYS138 4.6 33.4 1.0 CA D:CYS109 4.6 35.4 1.0 ND2 D:ASN111 4.7 32.9 1.0 CB D:TYR140 4.8 40.8 1.0 O D:HOH305 4.8 29.9 1.0 C D:TYR140 4.8 37.9 1.0 C D:CYS141 5.0 39.2 1.0

G.M.Cockrell, Y.Zheng, W.Guo, A.W.Peterson, J.K.Truong, E.R.Kantrowitz. New Paradigm For Allosteric Regulation of Escherichia Coli Aspartate Transcarbamoylase. Biochemistry V. 52 8036 2013.
ISSN: ISSN 0006-2960
PubMed: 24138583
DOI: 10.1021/BI401205N