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Zinc in PDB 3sau: Mutm Interrogation Complex 6

Enzymatic activity of Mutm Interrogation Complex 6

All present enzymatic activity of Mutm Interrogation Complex 6:
4.2.99.18;

Protein crystallography data

The structure of Mutm Interrogation Complex 6, PDB code: 3sau was solved by M.C.Spong, Y.Qi, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.25 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.423, 93.436, 104.920, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 21.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Mutm Interrogation Complex 6 (pdb code 3sau). 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 Interrogation Complex 6, PDB code: 3sau:

Zinc binding site 1 out of 1 in 3sau

Go back to Zinc Binding Sites List in 3sau
Zinc binding site 1 out of 1 in the Mutm Interrogation Complex 6


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutm Interrogation Complex 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:20.0
occ:1.00
SG A:CYS252 2.3 18.9 1.0
SG A:CYS249 2.3 20.1 1.0
SG A:CYS269 2.3 19.5 1.0
SG A:CYS272 3.0 31.4 1.0
CB A:CYS249 3.1 18.0 1.0
CB A:CYS252 3.4 23.4 1.0
CB A:CYS269 3.4 18.7 1.0
CB A:CYS272 3.7 27.4 1.0
N A:CYS252 3.8 19.6 1.0
CA A:CYS252 4.1 17.4 1.0
CE1 A:PHE182 4.2 20.9 1.0
N A:CYS272 4.3 23.4 1.0
CB A:ARG251 4.5 25.1 1.0
CA A:CYS249 4.6 22.1 1.0
C A:ARG251 4.7 21.1 1.0
CA A:CYS272 4.7 25.1 1.0
CB A:THR254 4.7 23.2 1.0
CB A:ARG271 4.7 20.5 1.0
CZ A:PHE182 4.7 20.9 1.0
C A:CYS252 4.8 21.6 1.0
CA A:CYS269 4.8 19.1 1.0
N A:GLY253 4.9 21.5 1.0
N A:THR254 5.0 22.3 1.0
CA A:ARG251 5.0 22.3 1.0
N A:ARG251 5.0 22.2 1.0
OG1 A:THR254 5.0 23.6 1.0

Reference:

Y.Qi, K.Nam, M.C.Spong, A.Banerjee, R.J.Sung, M.Zhang, M.Karplus, G.L.Verdine. Strandwise Translocation of A Dna Glycosylase on Undamaged Dna. Proc.Natl.Acad.Sci.Usa V. 109 1086 2012.
ISSN: ISSN 0027-8424
PubMed: 22219368
DOI: 10.1073/PNAS.1111237108
Page generated: Wed Dec 16 04:49:38 2020

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