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Crystal structure of mycobacterium tuberculosis uracil-DNA glycosylase, form IV

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

PDB: 4WRW
Type: protein
Length: 224 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uracil-DNA glycosylase
EC: 3.2.2.27
UniProt: P9WFQ9
Ligands: CL
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uracil-DNA glycosylase (EC 3.2.2.27)	protein	224	42% helix, 10% strand	P9WFQ9

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	131	0.50	0.80	35	CL, GOL
2	91	0.37	0.75	21	empty

Compared structures

4WRW · Crystal structure of Mycobacterium tuberculosis uracil-DNA glycosylase, Form IV · the same entry in another collection · chain A against A, TM-score 1.00
P9WFQ9 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P9WFQ9) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 4WRW · PDBe 4WRW · UniProt P9WFQ9

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