Atomistry » Zinc » PDB 1tnz-1u1j » 1tug
Atomistry »
  Zinc »
    PDB 1tnz-1u1j »
      1tug »

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy