Zinc in PDB 6kjb: Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167

All present enzymatic activity of Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167:
2.1.3.2;

The structure of Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167, PDB code: 6kjb was solved by N.Wang, Z.Lei, J.Zheng, Z.C.Jia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.56 / 2.06
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	129.680, 129.680, 197.980, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 22.3

The binding sites of Zinc atom in the Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167 (pdb code 6kjb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167, PDB code: 6kjb:

Zinc binding site 1 out of 1 in the Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Wild-Type Apo-Form E. Coli Atcase Holoenzyme with An Unusual Open Conformation of R167 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:23.8 occ:1.00 SG B:CYS141 2.3 23.1 1.0 SG B:CYS109 2.3 25.6 1.0 SG B:CYS114 2.4 22.4 1.0 SG B:CYS138 2.5 24.0 1.0 CB B:CYS114 3.1 22.7 1.0 CB B:CYS138 3.1 24.5 1.0 CB B:CYS141 3.1 22.7 1.0 CB B:CYS109 3.3 25.2 1.0 N B:CYS141 3.6 20.4 1.0 CA B:CYS141 3.9 22.0 1.0 CA B:CYS114 4.4 25.1 1.0 CB B:ASN111 4.5 26.1 1.0 OG B:SER116 4.5 28.4 1.0 ND2 B:ASN111 4.6 29.1 1.0 CA B:CYS138 4.6 27.1 1.0 CA B:CYS109 4.7 30.1 1.0 C B:TYR140 4.7 24.3 1.0 CB B:TYR140 4.8 23.8 1.0 C B:CYS141 4.8 26.4 1.0 O B:HOH345 4.9 28.4 1.0

Z.Lei, N.Wang, H.Tan, J.Zheng, Z.Jia. Conformational Plasticity of the Active Site Entrance Ine. Coliaspartate Transcarbamoylase and Its Implication in Feedback Regulation. Int J Mol Sci V. 21 2020.
ISSN: ESSN 1422-0067
PubMed: 31947715
DOI: 10.3390/IJMS21010320