Zinc in PDB 2a0f: Structure of D236A Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution

All present enzymatic activity of Structure of D236A Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution:
2.1.3.2;

The structure of Structure of D236A Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution, PDB code: 2a0f was solved by K.A.Stieglitz, K.J.Dusinberre, J.P.Cardia, H.Tsuruta, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.90
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.452, 120.452, 155.242, 90.00, 90.00, 120.00
R / Rfree (%)	21.7 / 27.9

The binding sites of Zinc atom in the Structure of D236A Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution (pdb code 2a0f). 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 Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution, PDB code: 2a0f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of D236A Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 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 Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:45.6 occ:1.00 SG B:CYS138 2.5 46.3 1.0 CB B:CYS138 2.6 42.3 1.0 SG B:CYS114 2.6 61.8 1.0 SG B:CYS141 2.6 56.8 1.0 SG B:CYS109 2.7 81.7 1.0 O B:HOH221 3.3 81.1 1.0 CB B:CYS114 3.4 62.4 1.0 OG B:SER116 3.4 60.3 1.0 CB B:CYS109 3.9 84.4 1.0 CE2 B:PHE125 4.0 66.8 1.0 CA B:CYS138 4.1 42.2 1.0 CB B:ASN111 4.3 79.0 1.0 CB B:CYS141 4.4 55.7 1.0 CB B:SER116 4.4 62.0 1.0 CD2 B:PHE125 4.7 67.0 1.0 N B:CYS141 4.7 52.1 1.0 C B:CYS138 4.8 41.3 1.0 O B:CYS138 4.8 40.5 1.0 N B:CYS138 4.8 43.6 1.0 CA B:CYS114 4.9 63.3 1.0 O B:ASN111 4.9 73.9 1.0 CZ B:PHE125 4.9 66.4 1.0 CG B:ASN111 5.0 80.2 1.0

Zinc binding site 2 out of 2 in the Structure of D236A Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 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 Mutant E. Coli Aspartate Transcarbamoylase in Presence of Phosphonoacetamide at 2.90 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:47.3 occ:1.00 CB D:CYS114 2.9 0.9 1.0 OG D:SER116 3.0 0.9 1.0 SG D:CYS138 3.3 0.5 1.0 O D:HOH174 3.3 43.7 1.0 SG D:CYS114 3.4 0.8 1.0 SG D:CYS109 3.8 0.6 1.0 O D:HOH156 3.9 89.9 1.0 CB D:TYR140 4.1 96.2 1.0 CB D:SER116 4.2 0.7 1.0 ND2 D:ASN111 4.3 0.1 1.0 O D:CYS114 4.3 0.2 1.0 CA D:CYS114 4.3 0.0 1.0 CB D:CYS141 4.4 99.8 1.0 N D:CYS141 4.5 96.5 1.0 CE2 D:PHE125 4.5 0.2 1.0 SG D:CYS141 4.6 0.0 1.0 N D:TYR140 4.6 97.6 1.0 CB D:ASN111 4.7 0.2 1.0 CE1 D:HIS117 4.7 0.2 1.0 CA D:TYR140 4.7 96.9 1.0 C D:CYS114 4.7 0.3 1.0 C D:TYR140 4.8 96.6 1.0 O D:ASN111 4.8 0.5 1.0 CB D:CYS109 4.9 0.8 1.0 CB D:CYS138 5.0 0.6 1.0 CG D:TYR140 5.0 95.0 1.0

K.A.Stieglitz, K.J.Dusinberre, J.P.Cardia, H.Tsuruta, E.R.Kantrowitz. Structure of the E.Coli Aspartate Transcarbamoylase Trapped in the Middle of the Catalytic Cycle. J.Mol.Biol. V. 352 478 2005.
ISSN: ISSN 0022-2836
PubMed: 16120448
DOI: 10.1016/J.JMB.2005.07.046