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Zinc in PDB 3c58: Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and A N7-Benzyl-Fapy-Dg Containing Dna

Enzymatic activity of Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and A N7-Benzyl-Fapy-Dg Containing Dna

All present enzymatic activity of Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and A N7-Benzyl-Fapy-Dg Containing Dna:
4.2.99.18;

Protein crystallography data

The structure of Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and A N7-Benzyl-Fapy-Dg Containing Dna, PDB code: 3c58 was solved by F.Coste, B.Castaing, T.Carell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.69 / 1.90
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.356, 91.356, 140.943, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 20

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 A N7-Benzyl-Fapy-Dg Containing Dna (pdb code 3c58). 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 A N7-Benzyl-Fapy-Dg Containing Dna, PDB code: 3c58:

Zinc binding site 1 out of 1 in 3c58

Go back to Zinc Binding Sites List in 3c58
Zinc binding site 1 out of 1 in the Crystal Structure of A Complex Between the Wild-Type Lactococcus Lactis Fpg (Mutm) and A N7-Benzyl-Fapy-Dg Containing Dna


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 A N7-Benzyl-Fapy-Dg Containing Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:6.6
occ:1.00
 SG A:CYS265 2.2 17.7 1.0
SG A:CYS245 2.3 19.2 1.0
SG A:CYS268 2.3 19.8 1.0
SG A:CYS248 2.4 18.1 1.0
CB A:CYS245 3.1 18.5 1.0
CB A:CYS268 3.3 19.1 1.0
CB A:CYS265 3.3 17.0 1.0
CB A:CYS248 3.3 23.3 1.0
N A:CYS268 3.8 17.5 1.0
N A:CYS248 3.9 24.4 1.0
CA A:CYS268 4.1 18.9 1.0
CA A:CYS248 4.2 23.8 1.0
CB A:VAL267 4.4 16.5 1.0
NE1 A:TRP179 4.4 17.3 1.0
CB A:ARG247 4.6 25.2 1.0
CA A:CYS245 4.6 21.1 1.0
CA A:CYS265 4.7 17.1 1.0
C A:VAL267 4.8 17.7 1.0
CG1 A:VAL267 4.8 15.5 1.0
C A:ARG247 4.8 26.0 1.0
C A:CYS248 4.8 24.2 1.0
N A:GLY249 4.9 23.2 1.0
NE A:ARG247 4.9 25.7 1.0
N A:ALA250 4.9 21.6 1.0
CB A:ALA250 4.9 20.0 1.0
NH2 A:ARG247 5.0 19.0 1.0

Reference:

F.Coste, M.Ober, Y.V.Le Bihan, M.A.Izquierdo, N.Hervouet, H.Mueller, T.Carell, B.Castaing. Bacterial Base Excision Repair Enzyme Fpg Recognizes Bulky N7-Substituted-Fapydg Lesion Via Unproductive Binding Mode Chem.Biol. V. 15 706 2008.
ISSN: ISSN 1074-5521
PubMed: 18635007
DOI: 10.1016/J.CHEMBIOL.2008.05.014
Page generated: Thu Oct 24 11:43:32 2024

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