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The crystal structure of alpha-D-glucuronidase from bacillus stearothermophilus T-1 complexed with glucuronic acid

Analyse The crystal structure of alpha-D-glucuronidase from bacillus stearothermophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MQQ
Type: protein
Length: 675 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-D-glucuronidase
EC: 3.2.1.139
UniProt: Q8VVD2
Ligands: GCU
Pockets: 5 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-D-glucuronidase (EC 3.2.1.139)	protein	675	39% helix, 13% strand	Q8VVD2

Ligands and binding sites

GCU · alpha-D-glucopyranuronic acid · sugar · chains A
GOL · Glycerol · additive · 11 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	119	0.57	0.84	26	GCU, GOL
2	199	0.49	0.76	33	empty
3	66	0.42	0.80	17	GOL
4	88	0.40	0.78	15	GOL
5	50	0.31	0.77	14	empty

Compared structures

1MQQ · The crystal structure of alpha-D-glucuronidase from bacillus stearothermophilus T-1… · the same entry in another collection · 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 Q8VVD2
Elsewhere: RCSB PDB 1MQQ · PDBe 1MQQ · UniProt Q8VVD2

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