Zinc in PDB 6kja: E. Coli Atcase Holoenzyme Mutant - G128/130A (Catalytic Chain)

All present enzymatic activity of E. Coli Atcase Holoenzyme Mutant - G128/130A (Catalytic Chain):
2.1.3.2;

The structure of E. Coli Atcase Holoenzyme Mutant - G128/130A (Catalytic Chain), PDB code: 6kja 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)	42.29 / 3.06
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	127.408, 127.408, 197.523, 90.00, 90.00, 120.00
R / Rfree (%)	24.9 / 28.3

The binding sites of Zinc atom in the E. Coli Atcase Holoenzyme Mutant - G128/130A (Catalytic Chain) (pdb code 6kja). 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 - G128/130A (Catalytic Chain), PDB code: 6kja:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the E. Coli Atcase Holoenzyme Mutant - G128/130A (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 - G128/130A (Catalytic Chain) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:58.3 occ:1.00 O B:HOH301 2.0 69.2 1.0 SG B:CYS109 2.3 49.6 1.0 SG B:CYS141 2.5 71.7 1.0 SG B:CYS114 2.5 60.1 1.0 SG B:CYS138 2.6 69.8 1.0 CB B:CYS138 3.2 57.5 1.0 CB B:CYS109 3.2 44.9 1.0 CB B:CYS114 3.4 57.6 1.0 CB B:CYS141 3.6 56.1 1.0 N B:CYS141 4.0 51.0 1.0 CA B:CYS141 4.4 53.3 1.0 OG B:SER116 4.6 58.3 1.0 CA B:CYS114 4.6 55.9 1.0 CA B:CYS109 4.6 53.0 1.0 CA B:CYS138 4.7 66.0 1.0 CB B:ASN111 4.7 47.4 1.0 ND2 B:ASN111 4.7 44.5 1.0 CB B:TYR140 5.0 47.6 1.0 CE2 B:PHE125 5.0 86.5 1.0

Zinc binding site 2 out of 3 in the E. Coli Atcase Holoenzyme Mutant - G128/130A (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 - G128/130A (Catalytic Chain) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:66.9 occ:1.00 SG D:CYS109 2.3 59.5 1.0 SG D:CYS141 2.4 48.1 1.0 SG D:CYS114 2.4 61.9 1.0 SG D:CYS138 2.5 53.2 1.0 CB D:CYS138 3.1 59.9 1.0 CB D:CYS114 3.3 66.0 1.0 CB D:CYS141 3.5 47.0 1.0 CB D:CYS109 3.5 66.3 1.0 N D:CYS141 3.9 55.3 1.0 CA D:CYS141 4.3 58.5 1.0 OG D:SER116 4.5 65.3 1.0 CA D:CYS138 4.6 69.7 1.0 CE2 D:PHE125 4.6 52.5 1.0 CA D:CYS114 4.7 52.4 1.0 CB D:TYR140 4.8 46.0 1.0 CB D:ASN111 4.8 52.3 1.0 CA D:CYS109 4.8 58.6 1.0 ND2 D:ASN111 4.8 55.3 1.0 C D:TYR140 5.0 56.8 1.0

Zinc binding site 3 out of 3 in the E. Coli Atcase Holoenzyme Mutant - G128/130A (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 - G128/130A (Catalytic Chain) within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn201 b:48.3 occ:1.00 SG F:CYS109 2.3 66.0 1.0 SG F:CYS141 2.3 44.0 1.0 SG F:CYS114 2.4 49.3 1.0 SG F:CYS138 2.5 46.4 1.0 CB F:CYS138 3.2 48.0 1.0 CB F:CYS114 3.3 42.4 1.0 CB F:CYS109 3.3 52.9 1.0 CB F:CYS141 3.4 45.8 1.0 N F:CYS141 3.8 62.8 1.0 CA F:CYS141 4.2 42.6 1.0 CA F:CYS114 4.6 47.4 1.0 OG F:SER116 4.6 42.1 1.0 CA F:CYS138 4.7 51.9 1.0 CB F:TYR140 4.7 42.2 1.0 CA F:CYS109 4.7 49.2 1.0 CB F:ASN111 4.8 50.4 1.0 ND2 F:ASN111 4.9 42.8 1.0 C F:TYR140 4.9 61.2 1.0 CE1 F:PHE125 5.0 42.8 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