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Zinc in PDB 3jr4: Mutm Interrogating An Extrahelical G

Enzymatic activity of Mutm Interrogating An Extrahelical G

All present enzymatic activity of Mutm Interrogating An Extrahelical G:
4.2.99.18;

Protein crystallography data

The structure of Mutm Interrogating An Extrahelical G, PDB code: 3jr4 was solved by Y.Qi, M.C.Spong, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.14 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.343, 95.377, 102.482, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 23.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Mutm Interrogating An Extrahelical G (pdb code 3jr4). 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 Mutm Interrogating An Extrahelical G, PDB code: 3jr4:

Zinc binding site 1 out of 1 in 3jr4

Go back to Zinc Binding Sites List in 3jr4
Zinc binding site 1 out of 1 in the Mutm Interrogating An Extrahelical G


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutm Interrogating An Extrahelical G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:26.3
occ:1.00
SG A:CYS272 2.4 22.9 1.0
SG A:CYS269 2.4 27.7 1.0
SG A:CYS249 2.4 27.4 1.0
SG A:CYS252 2.5 31.3 1.0
CB A:CYS249 3.2 29.2 1.0
CB A:CYS272 3.2 25.1 1.0
CB A:CYS269 3.4 27.2 1.0
CB A:CYS252 3.5 29.6 1.0
N A:CYS272 3.8 27.7 1.0
N A:CYS252 4.0 29.2 1.0
CA A:CYS272 4.1 26.3 1.0
CE1 A:PHE182 4.1 23.0 1.0
CA A:CYS252 4.3 30.2 1.0
CB A:ARG271 4.6 26.2 1.0
CZ A:PHE182 4.6 24.1 1.0
CA A:CYS249 4.6 30.4 1.0
CB A:ARG251 4.7 30.9 1.0
C A:ARG251 4.8 32.9 1.0
C A:ARG271 4.8 28.1 1.0
CB A:THR254 4.8 23.9 1.0
CA A:CYS269 4.8 25.9 1.0
OG1 A:THR254 4.9 25.9 1.0
C A:CYS252 4.9 31.4 1.0
N A:GLY253 4.9 26.1 1.0
N A:ARG251 5.0 27.8 1.0

Reference:

Y.Qi, M.C.Spong, K.Nam, M.Karplus, G.L.Verdine. Entrapment and Structure of An Extrahelical Guanine Attempting to Enter the Active Site of A Bacterial Dna Glycosylase, Mutm. J.Biol.Chem. V. 285 1468 2010.
ISSN: ISSN 0021-9258
PubMed: 19889642
DOI: 10.1074/JBC.M109.069799
Page generated: Sat Oct 26 07:29:53 2024

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