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Zinc in PDB 1tug: Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp)

Enzymatic activity of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp)

All present enzymatic activity of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp):
2.1.3.2;

Protein crystallography data

The structure of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp), PDB code: 1tug was solved by K.Stieglitz, B.Stec, D.P.Baker, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.10
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.290, 122.290, 142.410, 90.00, 90.00, 120.00
R / Rfree (%) 22 / 27.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp) (pdb code 1tug). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp), PDB code: 1tug:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1tug

Go back to Zinc Binding Sites List in 1tug
Zinc binding site 1 out of 2 in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn154

b:19.8
occ:1.00
SG B:CYS109 2.1 22.6 1.0
SG B:CYS114 2.3 14.3 1.0
SG B:CYS138 2.3 15.1 1.0
SG B:CYS141 2.4 16.5 1.0
CB B:CYS138 3.0 13.3 1.0
CB B:CYS114 3.2 33.1 1.0
CB B:CYS109 3.3 19.3 1.0
CB B:CYS141 3.4 15.7 1.0
N B:CYS141 3.7 11.8 1.0
CA B:CYS141 4.2 9.5 1.0
O B:HOH1159 4.4 16.9 1.0
CA B:CYS138 4.4 15.9 1.0
OG B:SER116 4.5 22.8 1.0
CA B:CYS114 4.5 28.9 1.0
ND2 B:ASN111 4.6 9.9 1.0
CA B:CYS109 4.7 20.9 1.0
CB B:ASN111 4.8 17.1 1.0
C B:CYS141 4.9 8.3 1.0
N B:GLU142 4.9 14.8 1.0
C B:CYS138 4.9 20.0 1.0
C B:TYR140 5.0 9.5 1.0

Zinc binding site 2 out of 2 in 1tug

Go back to Zinc Binding Sites List in 1tug
Zinc binding site 2 out of 2 in the Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5- Prime-Triphosphate (Ctp) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn155

b:0.0
occ:0.75
SG D:CYS114 0.8 34.2 1.0
CB D:CYS114 2.0 18.1 1.0
OG D:SER116 2.6 9.7 1.0
CA D:CYS114 2.8 12.2 1.0
SG D:CYS141 2.8 10.0 1.0
C D:CYS114 3.0 12.8 1.0
N D:ILE115 3.3 9.4 1.0
N D:SER116 3.3 23.1 1.0
CB D:SER116 3.6 12.1 1.0
SG D:CYS109 3.6 0.9 1.0
N D:CYS141 3.7 22.8 1.0
O D:CYS114 3.7 21.3 1.0
SG D:CYS138 3.7 14.8 1.0
CB D:CYS141 3.7 10.0 1.0
CB D:TYR140 3.9 13.4 1.0
CA D:CYS141 4.0 14.1 1.0
CA D:SER116 4.0 20.3 1.0
N D:CYS114 4.1 14.7 1.0
C D:ILE115 4.2 18.2 1.0
CA D:ILE115 4.3 7.8 1.0
O C:GLU109 4.4 15.9 1.0
ND1 D:HIS117 4.5 22.6 1.0
C D:TYR140 4.6 5.2 1.0
CB D:CYS109 4.6 1.1 1.0
C D:SER116 4.7 27.4 1.0
CG D:TYR140 4.7 18.6 1.0
CG2 D:ILE115 4.7 12.2 1.0
CD2 D:TYR140 4.8 22.0 1.0
CE1 D:HIS117 4.8 24.4 1.0
CA D:TYR140 4.8 6.5 1.0
N D:HIS117 4.9 26.3 1.0

Reference:

K.Stieglitz, B.Stec, D.P.Baker, E.R.Kantrowitz. Monitoring the Transition From the T to the R State in E.Coli Aspartate Transcarbamoylase By X-Ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States. J.Mol.Biol. V. 341 853 2004.
ISSN: ISSN 0022-2836
PubMed: 15288791
DOI: 10.1016/J.JMB.2004.06.002
Page generated: Wed Oct 16 19:17:53 2024

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