Zinc in PDB 1tu0: Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide

All present enzymatic activity of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide:
2.1.3.2;

The structure of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, PDB code: 1tu0 was solved by K.Stieglitz, B.Stec, D.P.Baker, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.55
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.200, 122.200, 142.700, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 27.9

The binding sites of Zinc atom in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide (pdb code 1tu0). 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 Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, PDB code: 1tu0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:19.8 occ:1.00 SG B:CYS141 2.1 10.3 1.0 SG B:CYS138 2.2 11.1 1.0 SG B:CYS109 2.2 23.8 1.0 SG B:CYS114 2.3 13.8 1.0 CB B:CYS138 2.8 4.7 1.0 CB B:CYS114 2.8 16.7 1.0 CB B:CYS141 3.1 19.9 1.0 CB B:CYS109 3.2 12.7 1.0 N B:CYS141 3.7 11.6 1.0 ND2 B:ASN111 3.9 15.2 1.0 CA B:CYS141 4.0 15.3 1.0 CA B:CYS114 4.1 15.1 1.0 CB B:ASN111 4.2 9.0 1.0 CA B:CYS138 4.3 9.7 1.0 CA B:CYS109 4.6 17.9 1.0 CG B:ASN111 4.6 9.9 1.0 C B:CYS141 4.7 14.9 1.0 O B:ASN111 4.8 14.8 1.0 CB B:TYR140 4.8 9.4 1.0 N B:GLU142 4.8 13.4 1.0 OG B:SER116 4.8 16.1 1.0 C B:TYR140 4.9 14.0 1.0 C B:CYS138 5.0 9.7 1.0 CB B:SER116 5.0 26.9 1.0 N B:CYS114 5.0 14.8 1.0

Zinc binding site 2 out of 2 in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn155 b:19.0 occ:1.00 SG D:CYS141 2.3 26.0 1.0 SG D:CYS114 2.4 8.8 1.0 SG D:CYS138 2.5 15.6 1.0 SG D:CYS109 2.5 20.7 1.0 CB D:CYS114 2.8 0.0 1.0 CB D:CYS141 3.1 9.9 1.0 CB D:CYS138 3.3 2.8 1.0 N D:CYS141 3.5 13.7 1.0 CB D:CYS109 3.6 19.8 1.0 CA D:CYS141 3.9 12.0 1.0 CA D:CYS114 4.1 2.0 1.0 CB D:ASN111 4.3 29.8 1.0 ND2 D:ASN111 4.5 14.8 1.0 CB D:TYR140 4.6 3.3 1.0 OG D:SER116 4.6 3.7 1.0 C D:TYR140 4.6 8.4 1.0 C D:CYS141 4.8 5.8 1.0 CA D:CYS138 4.8 12.2 1.0 N D:GLU142 4.9 3.0 1.0 O D:HOH164 4.9 27.4 1.0 CG D:ASN111 4.9 26.4 1.0 N D:TYR140 4.9 9.0 1.0 O D:ASN111 4.9 28.4 1.0 CA D:TYR140 5.0 0.0 1.0 CA D:CYS109 5.0 22.2 1.0

K.Stieglitz, B.Stec, D.P.Baker, E.R.Kantrowitz. Monitoring the Transition From the T to the R State in E.Coli Aspartate Transcarbamoylase By X-Ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States. J.Mol.Biol. V. 341 853 2004.
ISSN: ISSN 0022-2836
PubMed: 15288791
DOI: 10.1016/J.JMB.2004.06.002