Zinc in PDB 2ipo: E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine

All present enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine:
2.1.3.2;

The structure of E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine, PDB code: 2ipo was solved by J.P.Cardia, J.Eldo, J.Xia, E.M.O'day, 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 / 2.60
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.475, 120.475, 155.087, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 25.3

The binding sites of Zinc atom in the E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine (pdb code 2ipo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine, PDB code: 2ipo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:37.4 occ:1.00 SG B:CYS138 2.3 34.1 1.0 SG B:CYS141 2.3 34.5 1.0 SG B:CYS109 2.3 36.0 1.0 SG B:CYS114 2.4 35.0 1.0 CB B:CYS138 3.0 34.8 1.0 CB B:CYS141 3.1 34.2 1.0 CB B:CYS114 3.3 38.6 1.0 CB B:CYS109 3.3 38.9 1.0 N B:CYS141 3.5 30.5 1.0 CA B:CYS141 3.9 33.5 1.0 OG B:SER116 4.3 40.9 1.0 CB B:ASN111 4.4 39.6 1.0 CA B:CYS138 4.5 34.4 1.0 CB B:TYR140 4.6 29.4 1.0 CA B:CYS114 4.6 38.5 1.0 C B:TYR140 4.7 30.1 1.0 CA B:CYS109 4.8 40.7 1.0 O B:HOH224 4.8 32.8 1.0 C B:CYS141 4.8 34.2 1.0 ND2 B:ASN111 4.9 39.4 1.0 N B:GLU142 4.9 34.3 1.0 C B:CYS138 5.0 33.0 1.0 CA B:TYR140 5.0 29.2 1.0

Zinc binding site 2 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Aspartate Transcarbamoylase Complexed with N- Phosphonacetyl-L-Asparagine within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:38.9 occ:1.00 SG D:CYS138 2.3 37.1 1.0 SG D:CYS114 2.3 38.2 1.0 SG D:CYS109 2.4 39.4 1.0 SG D:CYS141 2.4 37.7 1.0 CB D:CYS138 3.1 38.8 1.0 CB D:CYS114 3.2 38.6 1.0 CB D:CYS109 3.2 39.3 1.0 CB D:CYS141 3.4 37.3 1.0 N D:CYS141 3.7 36.0 1.0 CA D:CYS141 4.2 37.9 1.0 OG D:SER116 4.3 37.7 1.0 CA D:CYS114 4.5 38.9 1.0 CA D:CYS138 4.5 39.2 1.0 CB D:ASN111 4.6 43.6 1.0 ND2 D:ASN111 4.6 42.5 1.0 CA D:CYS109 4.7 39.8 1.0 CB D:TYR140 4.7 34.5 1.0 C D:TYR140 4.9 36.2 1.0 C D:CYS141 5.0 38.7 1.0

J.P.Cardia, J.Eldo, J.Xia, E.M.O'day, H.Tsuruta, K.R.Gryncel, E.R.Kantrowitz. Use of L-Asparagine and N-Phosphonacetyl-L-Asparagine to Investigate the Linkage of Catalysis and Homotropic Cooperativity in E. Coli Aspartate Transcarbomoylase. Proteins V. 71 1088 2008.
ISSN: ISSN 0887-3585
PubMed: 18004787
DOI: 10.1002/PROT.21760