Zinc in PDB 1i5o: Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase

All present enzymatic activity of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase:
2.1.3.2;

The structure of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase, PDB code: 1i5o was solved by C.P.Macol, H.Tsuruta, 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 / 2.80
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.250, 122.250, 142.670, 90.00, 90.00, 120.00
R / Rfree (%)	15.5 / 21.2

The binding sites of Zinc atom in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase (pdb code 1i5o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase, PDB code: 1i5o:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn309 b:2.3 occ:1.00 SG B:CYS109 2.4 11.0 1.0 SG B:CYS138 2.4 14.9 1.0 SG B:CYS141 2.4 17.3 1.0 SG B:CYS114 2.4 18.7 1.0 CB B:CYS138 3.1 9.5 1.0 CB B:CYS114 3.1 17.6 1.0 CB B:CYS109 3.3 8.4 1.0 CB B:CYS141 3.3 11.3 1.0 N B:CYS141 3.6 7.7 1.0 CA B:CYS141 4.1 7.8 1.0 ND2 B:ASN111 4.3 16.0 1.0 OG B:SER116 4.4 7.3 1.0 CB B:ASN111 4.4 17.4 1.0 CA B:CYS114 4.5 13.9 1.0 CA B:CYS138 4.6 6.7 1.0 CB B:TYR140 4.6 8.4 1.0 C B:TYR140 4.7 6.1 1.0 CA B:CYS109 4.7 12.1 1.0 CG B:ASN111 4.9 19.4 1.0 C B:CYS141 4.9 6.2 1.0 CA B:TYR140 5.0 5.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn409 b:2.0 occ:1.00 SG D:CYS114 2.3 6.3 1.0 SG D:CYS138 2.3 6.2 1.0 SG D:CYS141 2.3 14.4 1.0 SG D:CYS109 2.4 28.9 1.0 CB D:CYS114 3.0 2.0 1.0 CB D:CYS138 3.1 17.5 1.0 CB D:CYS141 3.4 5.6 1.0 CB D:CYS109 3.4 5.3 1.0 N D:CYS141 3.5 6.2 1.0 OG D:SER116 4.0 15.3 1.0 CA D:CYS141 4.1 3.9 1.0 ND2 D:ASN111 4.1 23.2 1.0 CA D:CYS114 4.2 6.5 1.0 CB D:TYR140 4.4 6.9 1.0 CA D:CYS138 4.6 18.2 1.0 C D:TYR140 4.6 8.5 1.0 CB D:ASN111 4.7 23.5 1.0 O D:ASN111 4.8 18.6 1.0 CA D:TYR140 4.8 10.3 1.0 CB D:SER116 4.8 14.8 1.0 CA D:CYS109 4.9 4.7 1.0 CG D:ASN111 4.9 21.8 1.0 N D:TYR140 5.0 11.0 1.0

C.P.Macol, H.Tsuruta, B.Stec, E.R.Kantrowitz. Direct Structural Evidence For A Concerted Allosteric Transition in Escherichia Coli Aspartate Transcarbamoylase. Nat.Struct.Biol. V. 8 423 2001.
ISSN: ISSN 1072-8368
PubMed: 11323717
DOI: 10.1038/87582