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Zinc in PDB 6rok: The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor

Enzymatic activity of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor

All present enzymatic activity of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor:
3.2.2.23; 4.2.99.18;

Protein crystallography data

The structure of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor, PDB code: 6rok was solved by F.Coste, S.Goffinont, B.Castaing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.84 / 1.95
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.633, 91.633, 141.858, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 19.6

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor (pdb code 6rok). 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 The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor, PDB code: 6rok:

Zinc binding site 1 out of 1 in 6rok

Go back to Zinc Binding Sites List in 6rok
Zinc binding site 1 out of 1 in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:35.7
occ:1.00
 SG A:CYS265 2.1 29.9 1.0
SG A:CYS268 2.3 36.5 1.0
SG A:CYS248 2.4 33.9 1.0
SG A:CYS245 2.4 34.4 1.0
CB A:CYS245 3.2 34.6 1.0
CB A:CYS268 3.3 33.4 1.0
CB A:CYS265 3.3 27.9 1.0
CB A:CYS248 3.3 42.5 1.0
N A:CYS268 3.8 30.7 1.0
N A:CYS248 3.8 44.4 1.0
CA A:CYS248 4.1 43.6 1.0
CA A:CYS268 4.1 35.0 1.0
CB A:VAL267 4.4 33.7 1.0
NE1 A:TRP179 4.5 30.8 1.0
CB A:ARG247 4.5 41.2 1.0
CA A:CYS245 4.7 37.1 1.0
CA A:CYS265 4.7 34.2 1.0
C A:CYS248 4.7 43.4 1.0
N A:GLY249 4.8 39.4 1.0
CG1 A:VAL267 4.8 35.0 1.0
C A:ARG247 4.8 45.2 1.0
C A:VAL267 4.8 37.2 1.0
NE A:ARG247 4.9 40.1 1.0
N A:ARG247 4.9 41.1 1.0
N A:ALA250 4.9 36.2 1.0
CB A:ALA250 4.9 34.5 1.0
CA A:ARG247 5.0 43.0 1.0

Reference:

C.Rieux, S.Goffinont, F.Coste, Z.Tber, J.Cros, V.Roy, M.Guerin, V.Gaudon, S.Bourg, A.Biela, V.Aucagne, L.Agrofoglio, N.Garnier, B.Castaing. Thiopurine Derivative-Induced Fpg/Nei Dna Glycosylase Inhibition: Structural, Dynamic and Functional Insights. Int J Mol Sci V. 21 2020.
ISSN: ESSN 1422-0067
PubMed: 32192183
DOI: 10.3390/IJMS21062058
Page generated: Tue Oct 29 06:41:51 2024

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