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The crystal structure of uracil-DNA N-glycosylase (ung) from deinococcus radiodurans.

Analyse The crystal structure of uracil-DNA N-glycosylase (ung) from deinococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BOO
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uracil-DNA glycosylase
EC: 3.2.2.3
UniProt: Q9RWH9
Ligands: NO3
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uracil-DNA glycosylase (EC 3.2.2.3)	protein	230	40% helix, 11% strand	Q9RWH9

Ligands and binding sites

NO3 · Nitrate ion · ion · 3 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	174	0.51	0.78	34	NO3
2	130	0.45	0.77	20	NO3

Compared structures

2BOO · The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans. · the same entry in another collection · chain A against A, TM-score 1.00
Q9RWH9 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (Q9RWH9) · 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 Q9RWH9
Elsewhere: RCSB PDB 2BOO · PDBe 2BOO · UniProt Q9RWH9

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