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Zinc in PDB 1f1b: Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate

Enzymatic activity of Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate

All present enzymatic activity of Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate:
2.1.3.2;

Protein crystallography data

The structure of Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate, PDB code: 1f1b was solved by L.Jin, B.Stec, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.30
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.150, 122.150, 156.230, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 23.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate (pdb code 1f1b). 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 E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate, PDB code: 1f1b:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1f1b

Go back to Zinc Binding Sites List in 1f1b
Zinc binding site 1 out of 2 in the Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate


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 E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn313

b:22.8
occ:1.00
SG B:CYS114 2.3 18.0 1.0
SG B:CYS141 2.3 21.1 1.0
SG B:CYS138 2.3 24.5 1.0
SG B:CYS109 2.3 23.9 1.0
CB B:CYS138 2.9 23.0 1.0
CB B:CYS141 3.1 21.0 1.0
CB B:CYS114 3.3 22.6 1.0
CB B:CYS109 3.3 26.8 1.0
N B:CYS141 3.6 18.0 1.0
CA B:CYS141 3.9 20.9 1.0
OG B:SER116 4.1 10.8 1.0
CA B:CYS138 4.4 21.7 1.0
CA B:CYS114 4.6 19.2 1.0
CB B:ASN111 4.6 19.6 1.0
C B:CYS141 4.7 21.3 1.0
CA B:CYS109 4.7 31.4 1.0
ND2 B:ASN111 4.8 26.4 1.0
CB B:TYR140 4.8 13.9 1.0
C B:TYR140 4.8 19.7 1.0
N B:GLU142 4.8 18.0 1.0
CZ B:PHE145 5.0 56.4 1.0

Zinc binding site 2 out of 2 in 1f1b

Go back to Zinc Binding Sites List in 1f1b
Zinc binding site 2 out of 2 in the Crystal Structure of E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate


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 E. Coli Aspartate Transcarbamoylase P268A Mutant in the R-State in the Presence of N-Phosphonacetyl-L-Aspartate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn314

b:19.4
occ:1.00
SG D:CYS141 2.3 27.2 1.0
SG D:CYS114 2.3 21.7 1.0
SG D:CYS138 2.3 24.2 1.0
SG D:CYS109 2.3 24.4 1.0
CB D:CYS138 3.0 11.9 1.0
CB D:CYS114 3.1 16.4 1.0
CB D:CYS109 3.3 19.2 1.0
CB D:CYS141 3.4 22.2 1.0
N D:CYS141 3.7 22.1 1.0
CA D:CYS141 4.1 21.2 1.0
CB D:ASN111 4.4 27.6 1.0
CA D:CYS114 4.4 17.0 1.0
CA D:CYS138 4.5 19.0 1.0
CA D:CYS109 4.7 20.0 1.0
OG D:SER116 4.7 19.1 1.0
CB D:TYR140 4.8 19.9 1.0
C D:TYR140 4.9 20.1 1.0

Reference:

L.Jin, B.Stec, E.R.Kantrowitz. A Cis-Proline to Alanine Mutant of E. Coli Aspartate Transcarbamoylase: Kinetic Studies and Three-Dimensional Crystal Structures. Biochemistry V. 39 8058 2000.
ISSN: ISSN 0006-2960
PubMed: 10891088
DOI: 10.1021/BI000418+
Page generated: Sun Oct 13 00:37:27 2024

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