MolNFT v1 · #118191 · protein

Crystallographic and enzymatic studies of an active site variant H187Q of escherichia COLI uracil DNA glycosylase: crystal structures of mutant H187Q and its uracil complex

5EUG · Protein (glycosylase): “Crystallographic and enzymatic studies of an active site variant H187Q of escherichia COLI uracil DNA…”. X-ray diffraction, 1 ligand (URA), 1 pocket (best druggability 0.57). MolNFT v1 #118191 on GenesisL1…

PDB: 5EUG
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (glycosylase)
EC: 3.2.2.3
UniProt: P12295
Ligands: URA
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (glycosylase) (EC 3.2.2.3)	protein	225	39% helix, 11% strand	P12295

Ligands and binding sites

URA · Uracil · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.57	0.81	31	URA

Compared structures

5EUG · Crystallographic and enzymatic studies of an active site variant H187Q of escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
P12295 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P12295) · 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 P12295
Elsewhere: RCSB PDB 5EUG · PDBe 5EUG · UniProt P12295

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