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Crystal structure glucan 1,4-beta-glucosidase from saccharopolyspora erythraea

Analyse Crystal structure glucan 1,4-beta-glucosidase from saccharopolyspora erythraea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5M6G
Type: protein
Length: 579 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucosidase
EC: 3.2.1.74
UniProt: A4FNP6
Ligands: SOR, MG
Pockets: 2 · best druggability 0.52

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosidase (EC 3.2.1.74)	protein	579	39% helix, 13% strand	A4FNP6

Ligands and binding sites

SOR · sorbitol · ligand · chains A
MG · Magnesium ion · metal · 6 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
PGE · Triethylene glycol · additive · chains A

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

Pockets

2 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	112	0.52	0.82	23	SOR
2	72	0.32	0.75	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5M6G · Crystal structure Glucan 1,4-beta-glucosidase from Saccharopolyspora erythraea · 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 A4FNP6
Elsewhere: RCSB PDB 5M6G · PDBe 5M6G · UniProt A4FNP6

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