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Zinc in PDB 2xzu: Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K

Enzymatic activity of Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K

All present enzymatic activity of Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K:
3.2.2.23; 4.2.99.18;

Protein crystallography data

The structure of Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K, PDB code: 2xzu was solved by Y.V.Lebihan, M.A.Izquierdo, F.Coste, F.Culard, T.H.Gehrke, K.Essalhi, P.Aller, T.Carrel, B.Castaing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.079 / 1.82
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.739, 91.739, 143.236, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 18.87

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K (pdb code 2xzu). 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 Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K, PDB code: 2xzu:

Zinc binding site 1 out of 1 in 2xzu

Go back to Zinc Binding Sites List in 2xzu
Zinc binding site 1 out of 1 in the Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K


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 A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and An Oxidized Pyrimidine Containing Dna at 310K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:23.5
occ:1.00
 SG A:CYS265 2.2 21.3 1.0
SG A:CYS268 2.3 24.8 1.0
SG A:CYS248 2.3 22.5 1.0
SG A:CYS245 2.4 23.4 1.0
CB A:CYS245 3.1 24.4 1.0
CB A:CYS265 3.3 19.5 1.0
CB A:CYS268 3.4 20.2 1.0
CB A:CYS248 3.4 29.2 1.0
N A:CYS248 3.7 31.7 1.0
N A:CYS268 3.8 21.3 1.0
CA A:CYS248 4.1 33.1 1.0
CA A:CYS268 4.2 20.2 1.0
CB A:VAL267 4.4 20.5 1.0
NE1 A:TRP179 4.5 20.9 1.0
CB A:ARG247 4.5 31.2 1.0
CA A:CYS245 4.6 22.9 1.0
C A:ARG247 4.7 32.6 1.0
CA A:CYS265 4.8 21.3 1.0
C A:CYS248 4.8 32.8 1.0
N A:GLY249 4.8 29.5 1.0
C A:VAL267 4.8 21.9 1.0
CB A:ALA250 4.8 25.0 1.0
CG1 A:VAL267 4.9 22.8 1.0
NE A:ARG247 4.9 26.4 1.0
N A:ARG247 4.9 28.9 1.0
N A:ALA250 4.9 28.7 1.0
CA A:ARG247 5.0 31.2 1.0

Reference:

Y.V.Le Bihan, M.A.Izquierdo, F.Coste, P.Aller, F.Culard, T.H.Gehrke, K.Essalhi, T.Carrel, B.Castaing. 5-Hydroxy-5-Methylhydantoin Dna Lesion, A Molecular Trap For Dna Glycosylases Nucleic Acids Res. V. 39 6277 2011.
ISSN: ISSN 0305-1048
PubMed: 21486746
DOI: 10.1093/NAR/GKR215
Page generated: Thu Oct 17 05:37:44 2024

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