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Unsaturated glucuronyl hydrolase triggers hydration of vinyl ether group but not of glycosidic bond

Analyse Unsaturated glucuronyl hydrolase triggers hydration of vinyl ether group but… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2D5J
Type: protein
Length: 754 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Unsaturated glucuronyl hydrolase
EC: 3.2.1.-
UniProt: Q9RC92
Pockets: 4 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Unsaturated glucuronyl hydrolase (EC 3.2.1.-)	protein	377	54% helix, 10% strand	Q9RC92

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.41	0.78	21	empty
2	83	0.40	0.78	17	empty
3	149	0.39	0.73	28	empty
4	77	0.29	0.72	19	empty

Interfaces

1 interface between chains.

A–B · 948 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

2D5J · Unsaturated Glucuronyl Hydrolase Triggers Hydration of Vinyl Ether Group but not of… · the same entry in another collection · chain A against A, TM-score 1.00
Q9RC92 · AlphaFold monomer V2.0 prediction for unsaturated glucuronyl hydrolase (Q9RC92) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q9RC92
Elsewhere: RCSB PDB 2D5J · PDBe 2D5J · UniProt Q9RC92

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