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The crystal structure of alpha-D-glucuronidase (E386Q) from bacillus stearothermophilus T-6

Analyse The crystal structure of alpha-D-glucuronidase (E386Q) from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MQR
Type: protein
Length: 674 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: Q9ZFM3
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-D-glucuronidase (EC 3.2.1.139)	protein	674	39% helix, 12% strand	Q9ZFM3

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	350	0.70	0.83	45	empty
2	187	0.50	0.77	25	empty
3	162	0.48	0.77	27	empty
4	81	0.47	0.81	15	GOL
5	102	0.43	0.78	15	empty

Compared structures

1MQR · The crystal structure of alpha-D-glucuronidase (E386Q) from bacillus stearothermophilus… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9ZFM3
Elsewhere: RCSB PDB 1MQR · PDBe 1MQR · UniProt Q9ZFM3

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