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Zinc in PDB 7at1: Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H

Enzymatic activity of Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H

All present enzymatic activity of Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H:
2.1.3.2;

Protein crystallography data

The structure of Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H, PDB code: 7at1 was solved by J.E.Gouaux, R.C.Stevens, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.80
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.500, 122.500, 156.500, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H (pdb code 7at1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H, PDB code: 7at1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7at1

Go back to Zinc Binding Sites List in 7at1
Zinc binding site 1 out of 2 in the Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn154

b:35.1
occ:1.00
 SG B:CYS141 2.3 20.7 1.0
SG B:CYS109 2.3 26.2 1.0
SG B:CYS138 2.3 25.1 1.0
SG B:CYS114 2.4 20.3 1.0
CB B:CYS114 3.1 28.0 1.0
CB B:CYS138 3.2 25.7 1.0
CB B:CYS109 3.2 26.7 1.0
CB B:CYS141 3.3 23.8 1.0
N B:CYS141 3.7 22.1 1.0
CB B:ASN111 4.0 27.5 1.0
CA B:CYS141 4.1 21.9 1.0
OG B:SER116 4.2 25.7 1.0
CA B:CYS114 4.5 26.1 1.0
CA B:CYS138 4.6 25.6 1.0
ND2 B:ASN111 4.7 26.6 1.0
CA B:CYS109 4.7 29.1 1.0
CZ B:PHE145 4.8 39.3 1.0
C B:TYR140 4.8 21.4 1.0
CB B:TYR140 4.8 18.0 1.0
CG B:ASN111 4.8 26.2 1.0
C B:CYS141 4.9 23.5 1.0
N B:ASN111 4.9 31.4 1.0
O B:ASN111 5.0 34.4 1.0

Zinc binding site 2 out of 2 in 7at1

Go back to Zinc Binding Sites List in 7at1
Zinc binding site 2 out of 2 in the Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-Angstroms Resolution and Neutral P*H within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn154

b:30.0
occ:1.00
 SG D:CYS141 2.3 23.1 1.0
SG D:CYS114 2.3 25.6 1.0
SG D:CYS109 2.4 27.0 1.0
SG D:CYS138 2.4 25.5 1.0
CB D:CYS114 3.2 24.0 1.0
CB D:CYS109 3.2 23.7 1.0
CB D:CYS138 3.2 27.4 1.0
CB D:CYS141 3.3 21.2 1.0
N D:CYS141 3.7 17.1 1.0
CA D:CYS141 4.1 17.8 1.0
OG D:SER116 4.2 28.5 1.0
CB D:ASN111 4.2 24.9 1.0
ND2 D:ASN111 4.4 22.2 1.0
CA D:CYS114 4.4 22.6 1.0
CA D:CYS109 4.6 26.4 1.0
CA D:CYS138 4.7 24.1 1.0
CG D:ASN111 4.7 22.4 1.0
CB D:TYR140 4.8 21.3 1.0
C D:TYR140 4.9 19.8 1.0
O D:ASN111 4.9 26.4 1.0
C D:CYS141 5.0 19.7 1.0

Reference:

J.E.Gouaux, R.C.Stevens, W.N.Lipscomb. Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or Atp at 2.8-A Resolution and Neutral pH. Biochemistry V. 29 7702 1990.
ISSN: ISSN 0006-2960
PubMed: 2271529
DOI: 10.1021/BI00485A020
Page generated: Tue Oct 29 17:12:09 2024

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