Zinc in PDB 6kj8: E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain)

All present enzymatic activity of E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain):
2.1.3.2;

The structure of E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain), PDB code: 6kj8 was solved by 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)	47.87 / 3.01
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	126.592, 126.592, 196.490, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 24.7

The binding sites of Zinc atom in the E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain) (pdb code 6kj8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain), PDB code: 6kj8:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:47.2 occ:1.00 SG B:CYS141 2.2 50.2 1.0 SG B:CYS114 2.3 48.2 1.0 SG B:CYS109 2.4 45.4 1.0 SG B:CYS138 2.5 50.8 1.0 CB B:CYS138 3.1 51.6 1.0 CB B:CYS109 3.2 46.9 1.0 CB B:CYS114 3.3 49.0 1.0 CB B:CYS141 3.4 49.4 1.0 N B:CYS141 3.9 48.8 1.0 CA B:CYS141 4.2 48.2 1.0 CA B:CYS114 4.5 49.7 1.0 CB B:ASN111 4.6 47.5 1.0 CA B:CYS109 4.6 48.0 1.0 CA B:CYS138 4.6 53.0 1.0 ND2 B:ASN111 4.8 49.0 1.0 CE2 B:PHE125 4.9 50.9 1.0 CB B:TYR140 4.9 44.6 1.0 OG B:SER116 4.9 49.1 1.0 C B:CYS141 5.0 46.2 1.0 O B:ASN111 5.0 49.3 1.0

Zinc binding site 2 out of 3 in the E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:56.5 occ:1.00 SG D:CYS109 2.3 56.6 1.0 SG D:CYS114 2.4 50.3 1.0 SG D:CYS138 2.5 54.4 1.0 SG D:CYS141 2.5 42.7 1.0 CB D:CYS138 3.2 54.5 1.0 CB D:CYS109 3.2 54.6 1.0 CB D:CYS114 3.3 51.3 1.0 CB D:CYS141 3.5 43.7 1.0 N D:CYS141 3.9 47.4 1.0 CA D:CYS141 4.3 47.1 1.0 CA D:CYS114 4.5 50.1 1.0 CA D:CYS109 4.6 51.6 1.0 OG D:SER116 4.6 42.5 1.0 CE1 D:PHE125 4.6 56.4 1.0 CA D:CYS138 4.7 53.4 1.0 CB D:ASN111 4.7 50.4 1.0

Zinc binding site 3 out of 3 in the E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of E. Coli Atcase Holoenzyme Mutant - G166P (Catalytic Chain) within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn201 b:39.2 occ:1.00 SG F:CYS109 2.2 45.0 1.0 SG F:CYS141 2.3 40.7 1.0 SG F:CYS114 2.4 36.8 1.0 SG F:CYS138 2.4 41.0 1.0 CB F:CYS138 3.1 43.8 1.0 CB F:CYS109 3.3 42.4 1.0 CB F:CYS114 3.3 38.3 1.0 CB F:CYS141 3.4 40.3 1.0 N F:CYS141 3.8 43.2 1.0 CA F:CYS141 4.2 39.8 1.0 CA F:CYS114 4.6 38.9 1.0 CA F:CYS109 4.6 39.3 1.0 CB F:ASN111 4.6 42.6 1.0 CA F:CYS138 4.7 44.2 1.0 CB F:SER116 4.7 46.9 1.0 CB F:TYR140 4.8 39.0 1.0 ND2 F:ASN111 4.9 45.0 1.0 C F:TYR140 5.0 44.1 1.0

Z.Lei, B.Wang, Z.Lu, N.Wang, H.Tan, J.Zheng, Z.Jia. New Regulatory Mechanism-Based Inhibitors of Aspartate Transcarbamoylase For Potential Anticancer Drug Development. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 31967710
DOI: 10.1111/FEBS.15220