Zinc in PDB 2hse: Structure of D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution

All present enzymatic activity of Structure of D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution:
2.1.3.2;

The structure of Structure of D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution, PDB code: 2hse was solved by J.Wang, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.076, 121.076, 155.235, 90.00, 90.00, 120.00
R / Rfree (%)	20.9 / 25.4

The binding sites of Zinc atom in the Structure of D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution (pdb code 2hse). 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 D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution, PDB code: 2hse:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A 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 D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn954 b:53.5 occ:1.00 SG B:CYS141 2.3 51.4 1.0 SG B:CYS138 2.3 54.8 1.0 SG B:CYS109 2.3 53.8 1.0 SG B:CYS114 2.4 52.8 1.0 O B:HOH155 2.7 78.5 1.0 CB B:CYS138 3.1 53.1 1.0 CB B:CYS141 3.2 51.8 1.0 CB B:CYS114 3.3 51.6 1.0 CB B:CYS109 3.3 55.2 1.0 N B:CYS141 3.7 47.8 1.0 CA B:CYS141 4.1 51.0 1.0 OG B:SER116 4.2 55.9 1.0 CB B:ASN111 4.5 53.8 1.0 ND2 B:ASN111 4.5 48.8 1.0 CA B:CYS138 4.6 53.6 1.0 CA B:CYS114 4.6 51.0 1.0 CA B:CYS109 4.7 58.4 1.0 CB B:TYR140 4.7 44.8 1.0 C B:TYR140 4.8 47.1 1.0 C B:CYS141 4.9 52.3 1.0 CG B:ASN111 5.0 52.6 1.0

Zinc binding site 2 out of 2 in the Structure of D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A 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 D236A E. Coli Aspartate Transcarbamoylase in the Presence of Phosphonoacetamide and L-Aspartate at 2.60 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn955 b:80.3 occ:1.00 SG D:CYS114 2.3 78.9 1.0 SG D:CYS138 2.3 80.6 1.0 SG D:CYS109 2.3 83.0 1.0 SG D:CYS141 2.4 82.0 1.0 CB D:CYS138 3.0 83.1 1.0 CB D:CYS114 3.2 75.7 1.0 CB D:CYS109 3.3 83.3 1.0 CB D:CYS141 3.3 77.9 1.0 N D:CYS141 3.7 76.7 1.0 CA D:CYS141 4.1 78.1 1.0 OG D:SER116 4.1 71.5 1.0 ND2 D:ASN111 4.4 72.8 1.0 CA D:CYS114 4.5 74.6 1.0 CA D:CYS138 4.5 83.4 1.0 CB D:TYR140 4.7 76.0 1.0 CA D:CYS109 4.8 83.8 1.0 C D:TYR140 4.8 76.2 1.0 CB D:ASN111 4.8 75.7 1.0 C D:CYS141 4.9 78.9 1.0 N D:TYR140 5.0 76.9 1.0 N D:GLU142 5.0 79.4 1.0

J.Wang, J.Eldo, E.R.Kantrowitz. The Allosteric Transition Induced By the Aspartate Binding to Aspartate Transcarbamoylase To Be Published.