Zinc in PDB 7icq: Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2

Protein crystallography data

The structure of Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2, PDB code: 7icq was solved by H.Pelletier, M.R.Sawaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 178.939, 57.796, 48.486, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / n/a

Other elements in 7icq:

The structure of Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2 also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2 (pdb code 7icq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2, PDB code: 7icq:

Zinc binding site 1 out of 1 in 7icq

Go back to Zinc Binding Sites List in 7icq
Zinc binding site 1 out of 1 in the Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dna Polymerase Beta (E.C.2.7.7.7)/Dna Complex, Soaked in the Presence of ZNCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn343

b:93.4
occ:1.00
ND1 A:HIS51 2.9 45.7 1.0
CG A:HIS51 3.5 45.3 1.0
CB A:HIS51 3.7 44.6 1.0
CE1 A:HIS51 3.7 42.6 1.0
CA A:HIS51 4.3 36.7 1.0
CD2 A:HIS51 4.4 42.0 1.0
N A:LYS52 4.5 35.7 1.0
NE2 A:HIS51 4.5 40.1 1.0
C A:HIS51 5.0 38.3 1.0

Reference:

H.Pelletier, M.R.Sawaya, W.Wolfle, S.H.Wilson, J.Kraut. A Structural Basis For Metal Ion Mutagenicity and Nucleotide Selectivity in Human Dna Polymerase Beta Biochemistry V. 35 12762 1996.
ISSN: ISSN 0006-2960
PubMed: 8841119
DOI: 10.1021/BI9529566
Page generated: Tue Oct 29 20:52:38 2024

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