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Crystal structure of Mycobacterium tuberculosis Uracil-DNA glycosylase in complex with 6-Formyl-uracil, Form III

Analyse Crystal structure of Mycobacterium tuberculosis Uracil-DNA glycosylase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8I6C
Type: protein
Length: 227 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.28
Source: Mycobacterium tuberculosis H37Rv
Molecule: Uracil-DNA glycosylase
EC: 3.2.2.27
UniProt: P9WFQ9
Ligands: OG6
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · resolution 2.28 · 1 distinct chain · 43% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uracil-DNA glycosylase (EC 3.2.2.27)	protein	227	43% helix, 10% strand	P9WFQ9

Ligands and binding sites

OG6 · 6-[bis(oxidanyl)methyl]-5~{H}-pyrimidine-2,4-dione · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.45	0.78	27	OG6

Compared structures

P9WFQ9 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P9WFQ9) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P9WFQ9
Elsewhere: RCSB PDB 8I6C · PDBe 8I6C · UniProt P9WFQ9

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