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

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

The structure of The R State Structure of E. Coli Atcase with Atp Bound, PDB code: 4kgv 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)	38.40 / 2.10
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.070, 121.070, 155.490, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 20.7

The binding sites of Zinc atom in the The R State Structure of E. Coli Atcase with Atp Bound (pdb code 4kgv). 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 Atp Bound, PDB code: 4kgv:
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 Atp 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 Atp Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:36.7 occ:1.00 SG B:CYS141 2.3 34.2 1.0 SG B:CYS109 2.3 35.9 1.0 SG B:CYS138 2.4 32.7 1.0 SG B:CYS114 2.4 32.7 1.0 CB B:CYS114 3.1 29.6 1.0 CB B:CYS138 3.1 31.9 1.0 CB B:CYS109 3.2 34.1 1.0 CB B:CYS141 3.3 29.8 1.0 N B:CYS141 3.7 32.8 1.0 CA B:CYS141 4.0 35.9 1.0 OG B:SER116 4.3 34.1 1.0 CA B:CYS114 4.4 35.6 1.0 CB B:ASN111 4.5 41.9 1.0 CA B:CYS138 4.6 31.8 1.0 CA B:CYS109 4.7 37.8 1.0 ND2 B:ASN111 4.7 37.6 1.0 O B:HOH319 4.7 37.0 1.0 CB B:TYR140 4.8 28.9 1.0 C B:TYR140 4.8 31.2 1.0 C B:CYS141 4.9 30.1 1.0

Zinc binding site 2 out of 2 in the The R State Structure of E. Coli Atcase with Atp 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 Atp Bound within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:42.3 occ:1.00 SG D:CYS138 2.3 40.8 1.0 SG D:CYS114 2.3 39.2 1.0 SG D:CYS141 2.4 39.6 1.0 SG D:CYS109 2.4 40.7 1.0 CB D:CYS138 3.1 41.5 1.0 CB D:CYS109 3.2 37.8 1.0 CB D:CYS114 3.2 40.1 1.0 CB D:CYS141 3.3 35.8 1.0 N D:CYS141 3.7 44.2 1.0 CA D:CYS141 4.1 43.2 1.0 OG D:SER116 4.3 40.8 1.0 CA D:CYS114 4.5 39.4 1.0 CB D:ASN111 4.5 42.3 1.0 CA D:CYS109 4.6 43.3 1.0 CA D:CYS138 4.6 41.2 1.0 O D:HOH316 4.7 37.6 1.0 ND2 D:ASN111 4.7 34.5 1.0 CB D:TYR140 4.8 43.4 1.0 C D:TYR140 4.9 48.4 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