Zinc in PDB 1nbe: Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A)

All present enzymatic activity of Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A):
2.1.3.2;

The structure of Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A), PDB code: 1nbe was solved by M.K.Williams, B.Stec, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.60
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.470, 122.470, 142.770, 90.00, 90.00, 120.00
R / Rfree (%)	17.7 / 23.7

The binding sites of Zinc atom in the Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A) (pdb code 1nbe). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A), PDB code: 1nbe:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:11.1 occ:1.00 SG B:CYS138 2.3 2.0 1.0 SG B:CYS114 2.3 10.1 1.0 SG B:CYS109 2.4 2.0 1.0 SG B:CYS141 2.4 9.3 1.0 CB B:CYS138 2.9 11.6 1.0 CB B:CYS141 3.2 7.2 1.0 CB B:CYS114 3.3 12.8 1.0 CB B:CYS109 3.4 5.2 1.0 N B:CYS141 3.6 2.0 1.0 CA B:CYS141 4.0 5.2 1.0 CB B:ASN111 4.3 12.3 1.0 CA B:CYS138 4.4 10.2 1.0 CA B:CYS114 4.6 11.6 1.0 ND2 B:ASN111 4.7 21.2 1.0 C B:TYR140 4.7 4.2 1.0 C B:CYS141 4.7 2.8 1.0 CB B:TYR140 4.7 6.7 1.0 CA B:CYS109 4.8 9.0 1.0 OG B:SER116 4.8 11.2 1.0 CG B:ASN111 4.9 13.8 1.0 C B:CYS138 4.9 11.0 1.0 N B:GLU142 4.9 7.0 1.0 N B:TYR140 4.9 7.8 1.0 O B:CYS138 5.0 11.4 1.0

Zinc binding site 2 out of 2 in the Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamoylase Regulatory Chain Mutant (T82A) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:17.5 occ:1.00 SG D:CYS109 2.3 3.2 1.0 SG D:CYS138 2.3 6.0 1.0 SG D:CYS141 2.3 7.1 1.0 SG D:CYS114 2.3 2.7 1.0 CB D:CYS138 3.0 9.0 1.0 CB D:CYS114 3.1 2.1 1.0 CB D:CYS109 3.2 5.9 1.0 CB D:CYS141 3.5 9.0 1.0 N D:CYS141 3.7 2.4 1.0 CA D:CYS141 4.1 4.8 1.0 CB D:ASN111 4.3 9.3 1.0 CA D:CYS114 4.4 2.0 1.0 CA D:CYS138 4.5 9.6 1.0 CA D:CYS109 4.5 6.2 1.0 ND2 D:ASN111 4.5 18.5 1.0 OG D:SER116 4.6 6.3 1.0 C D:TYR140 4.9 4.4 1.0 C D:CYS141 4.9 5.9 1.0 CG D:ASN111 4.9 17.3 1.0 CB D:TYR140 4.9 10.8 1.0 N D:GLU142 5.0 6.4 1.0

M.K.Williams, B.Stec, E.R.Kantrowitz. A Single Mutation in the Regulatory Chain of Escherichia Coli Aspartate Transcarbamoylase Results in An Extreme T-State Structure. J.Mol.Biol. V. 281 121 1998.
ISSN: ISSN 0022-2836
PubMed: 9680480
DOI: 10.1006/JMBI.1998.1923