Zinc in PDB 2h3e: Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution

All present enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution:
2.1.3.2;

The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution, PDB code: 2h3e was solved by J.Eldo, J.P.Cardia, E.M.O'day, J.Xia, H.Tsuruta, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.41 / 2.30
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.320, 120.320, 154.510, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 25

The binding sites of Zinc atom in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution (pdb code 2h3e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution, PDB code: 2h3e:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn159 b:38.5 occ:1.00 SG B:CYS141 2.3 39.4 1.0 SG B:CYS109 2.3 36.5 1.0 SG B:CYS114 2.4 33.7 1.0 SG B:CYS138 2.4 37.6 1.0 CB B:CYS141 2.8 38.6 1.0 CB B:CYS138 3.1 35.5 1.0 CB B:CYS114 3.2 33.1 1.0 CB B:CYS109 3.3 37.0 1.0 N B:CYS141 3.6 35.4 1.0 CA B:CYS141 3.7 37.5 1.0 OG B:SER116 4.4 36.2 1.0 CB B:ASN111 4.5 33.5 1.0 CA B:CYS114 4.6 31.8 1.0 CA B:CYS138 4.6 37.1 1.0 CA B:CYS109 4.7 36.9 1.0 O B:HOH176 4.7 31.9 1.0 CB B:TYR140 4.8 32.1 1.0 C B:TYR140 4.8 33.9 1.0 ND2 B:ASN111 4.8 30.8 1.0

Zinc binding site 2 out of 2 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of N-Phosphonacetyl-L-Isoasparagine at 2.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn159 b:36.7 occ:1.00 SG D:CYS138 2.3 35.0 1.0 SG D:CYS141 2.3 34.2 1.0 SG D:CYS114 2.3 34.1 1.0 SG D:CYS109 2.4 34.6 1.0 CB D:CYS138 3.1 37.1 1.0 CB D:CYS114 3.2 34.6 1.0 CB D:CYS109 3.3 36.2 1.0 CB D:CYS141 3.3 35.2 1.0 N D:CYS141 3.6 35.3 1.0 CA D:CYS141 4.1 36.0 1.0 OG D:SER116 4.3 37.6 1.0 CA D:CYS114 4.5 34.9 1.0 CA D:CYS138 4.6 36.4 1.0 CB D:TYR140 4.7 33.6 1.0 ND2 D:ASN111 4.7 35.2 1.0 CA D:CYS109 4.7 37.4 1.0 CB D:ASN111 4.7 37.3 1.0 C D:TYR140 4.8 35.2 1.0 O D:HOH188 4.8 45.5 1.0 C D:CYS141 4.9 35.9 1.0

J.Eldo, J.P.Cardia, E.M.O'day, J.Xia, H.Tsuruta, E.R.Kantrowitz. N-Phosphonacetyl-L-Isoasparagine A Potent and Specific Inhibitor of Escherichia Coli Aspartate Transcarbamoylase. J.Med.Chem. V. 49 5932 2006.
ISSN: ISSN 0022-2623
PubMed: 17004708
DOI: 10.1021/JM0607294