Research workbench

G:T/U mismatch-specific DNA glycosylase from E.COLI

Analyse G:T/U mismatch-specific DNA glycosylase from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MUG
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (G:T/U specific DNA glycosylase)
EC: 3.2.2.-
UniProt: P0A9H1
Ligands: SO4
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (G:T/U specific DNA glycosylase) (EC 3.2.2.-)	protein	165	40% helix, 18% strand	P0A9H1

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	299	0.66	0.82	44	SO4

Compared structures

1MUG · G:T/U mismatch-specific DNA glycosylase from E.COLI · the same entry in another collection · chain A against A, TM-score 1.00
P0A9H1 · AlphaFold monomer V2.0 prediction for G/U mismatch-specific DNA glycosylase (P0A9H1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0A9H1
Elsewhere: RCSB PDB 1MUG · PDBe 1MUG · UniProt P0A9H1

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