Zinc in PDB 2air: T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme

All present enzymatic activity of T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme:
2.1.3.2;

The structure of T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme, PDB code: 2air was solved by J.Huang, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	129.152, 129.152, 198.097, 90.00, 90.00, 120.00
R / Rfree (%)	23.9 / 27.3

The binding sites of Zinc atom in the T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme (pdb code 2air). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme, PDB code: 2air:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn800 b:32.2 occ:1.00 SG B:CYS114 2.3 33.8 1.0 SG B:CYS138 2.4 32.4 1.0 SG B:CYS141 2.4 33.6 1.0 SG B:CYS109 2.4 38.6 1.0 CB B:CYS138 3.0 38.5 1.0 CB B:CYS114 3.1 31.2 1.0 CB B:CYS141 3.3 35.2 1.0 CB B:CYS109 3.3 39.0 1.0 N B:CYS141 3.7 37.8 1.0 CA B:CYS141 4.1 36.7 1.0 CA B:CYS114 4.4 32.4 1.0 CB B:ASN111 4.5 39.9 1.0 CA B:CYS138 4.5 40.2 1.0 ND2 B:ASN111 4.6 38.4 1.0 O B:HOH827 4.7 46.6 1.0 CB B:TYR140 4.7 38.8 1.0 CA B:CYS109 4.7 40.5 1.0 C B:TYR140 4.8 38.7 1.0 C B:CYS141 4.9 37.5 1.0 N B:GLU142 4.9 37.9 1.0

Zinc binding site 2 out of 2 in the T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of T-State Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn801 b:35.1 occ:1.00 SG H:CYS141 2.2 35.9 1.0 SG H:CYS109 2.3 39.7 1.0 SG H:CYS114 2.4 37.8 1.0 SG H:CYS138 2.4 40.2 1.0 CB H:CYS138 3.0 40.3 1.0 CB H:CYS114 3.2 33.8 1.0 CB H:CYS141 3.3 33.5 1.0 CB H:CYS109 3.4 42.4 1.0 N H:CYS141 3.6 34.2 1.0 CA H:CYS141 4.0 35.4 1.0 CB H:ASN111 4.5 35.7 1.0 CA H:CYS114 4.5 36.5 1.0 CA H:CYS138 4.5 41.0 1.0 O H:HOH823 4.6 39.5 1.0 CB H:TYR140 4.6 35.0 1.0 OG H:SER116 4.7 35.5 1.0 ND2 H:ASN111 4.7 35.2 1.0 CA H:CYS109 4.7 40.7 1.0 C H:TYR140 4.7 34.9 1.0 C H:CYS141 4.9 35.5 1.0 N H:GLU142 4.9 37.5 1.0

J.Huang, W.N.Lipscomb. T-State Active Site of Aspartate Transcarbamylase: Crystal Structure of the Carbamyl Phosphate and L-Alanosine Ligated Enzyme Biochemistry V. 45 346 2006.
ISSN: ISSN 0006-2960
PubMed: 16401065
DOI: 10.1021/BI051543U