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Crystal structure of the udp-glucuronic acid binding domain of the human drug metabolizing udp-glucuronosyltransferase 2B7

Analyse Crystal structure of the udp-glucuronic acid binding domain of the human drug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O6L
Type: protein
Length: 328 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-glucuronosyltransferase 2B7
EC: 2.4.1.17
UniProt: P16662
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucuronosyltransferase 2B7 (EC 2.4.1.17)	protein	162	41% helix, 16% strand	P16662
B	Udp-glucuronosyltransferase 2B7 (EC 2.4.1.17)	protein	166	42% helix, 16% strand	P16662

Pockets

3 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	219	0.54	0.77	21	empty
2	97	0.50	0.82	17	empty
3	51	0.31	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 709 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

2O6L · Crystal Structure of the UDP-Glucuronic Acid Binding Domain of the Human Drug… · the same entry in another collection · chain A against A, TM-score 1.00
P16662 · AlphaFold monomer V2.0 prediction for udp-glucuronosyltransferase 2B7 (P16662) · a predicted model of the same protein · chain B 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 P16662
Elsewhere: RCSB PDB 2O6L · PDBe 2O6L · UniProt P16662

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