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Crystal structure of human uracil-DNA glycosylase D183G/K302R mutant

Analyse Crystal structure of human uracil-DNA glycosylase D183G/K302R mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TKB
Type: protein
Length: 223 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: P13051
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uracil-DNA glycosylase (EC 3.2.2.27)	protein	223	41% helix, 11% strand	P13051

Ligands and binding sites

IMD · Imidazole · additive · 2 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	145	0.51	0.80	31	empty
2	63	0.35	0.77	13	empty

Compared structures

3TKB · crystal structure of human uracil-DNA glycosylase D183G/K302R mutant · the same entry in another collection · chain A against A, TM-score 1.00
P13051 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P13051) · 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 P13051
Elsewhere: RCSB PDB 3TKB · PDBe 3TKB · UniProt P13051

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