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Zinc in PDB 1rah: Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity

Enzymatic activity of Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity

All present enzymatic activity of Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity:
2.1.3.2;

Protein crystallography data

The structure of Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity, PDB code: 1rah was solved by R.P.Kosman, J.E.Gouaux, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.130, 122.130, 142.510, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity (pdb code 1rah). 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 Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity, PDB code: 1rah:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1rah

Go back to Zinc Binding Sites List in 1rah
Zinc binding site 1 out of 2 in the Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn154

b:22.5
occ:1.00
 SG B:CYS141 2.3 13.6 1.0
SG B:CYS114 2.3 17.4 1.0
SG B:CYS138 2.3 9.7 1.0
SG B:CYS109 2.3 16.1 1.0
CB B:CYS138 3.0 12.5 1.0
CB B:CYS109 3.1 13.6 1.0
CB B:CYS114 3.2 15.5 1.0
CB B:CYS141 3.4 10.8 1.0
N B:CYS141 3.9 16.0 1.0
CA B:CYS141 4.3 13.6 1.0
OG B:SER116 4.4 11.4 1.0
CB B:ASN111 4.5 9.2 1.0
CA B:CYS109 4.5 16.8 1.0
CA B:CYS138 4.5 14.4 1.0
ND2 B:ASN111 4.6 11.4 1.0
CA B:CYS114 4.7 16.2 1.0
O B:HOH1000 4.7 31.1 1.0
CB B:TYR140 4.9 10.8 1.0
C B:TYR140 5.0 11.0 1.0

Zinc binding site 2 out of 2 in 1rah

Go back to Zinc Binding Sites List in 1rah
Zinc binding site 2 out of 2 in the Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 Angstroms Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn154

b:20.7
occ:1.00
 SG D:CYS141 2.3 14.2 1.0
SG D:CYS109 2.3 17.9 1.0
SG D:CYS114 2.3 10.1 1.0
SG D:CYS138 2.3 10.4 1.0
CB D:CYS138 3.1 10.2 1.0
CB D:CYS109 3.1 14.1 1.0
CB D:CYS114 3.2 10.1 1.0
CB D:CYS141 3.4 6.2 1.0
N D:CYS141 3.8 9.7 1.0
CA D:CYS141 4.1 8.2 1.0
CB D:ASN111 4.4 17.8 1.0
OG D:SER116 4.4 15.3 1.0
CA D:CYS109 4.4 13.5 1.0
CA D:CYS114 4.5 9.6 1.0
CA D:CYS138 4.6 9.6 1.0
ND2 D:ASN111 4.6 17.2 1.0
CB D:TYR140 4.7 5.6 1.0
C D:TYR140 4.9 6.3 1.0
O D:HOH1004 4.9 15.6 1.0

Reference:

R.P.Kosman, J.E.Gouaux, W.N.Lipscomb. Crystal Structure of Ctp-Ligated T State Aspartate Transcarbamoylase at 2.5 A Resolution: Implications For Atcase Mutants and the Mechanism of Negative Cooperativity. Proteins V. 15 147 1993.
ISSN: ISSN 0887-3585
PubMed: 8441751
DOI: 10.1002/PROT.340150206
Page generated: Wed Oct 16 18:32:18 2024

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