MolNFT v1 · #114661 · protein

Crystal structure of the beta-glucosidase from trichoderma harzianum

5BWF · Beta-1,4-glucosidase: “Crystal structure of the beta-glucosidase from trichoderma harzianum”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.76). MolNFT v1 #114661 on GenesisL1: 3D structure, binding sites and…

PDB: 5BWF
Type: protein
Length: 942 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-1,4-glucosidase
UniProt: A3FPG4
Ligands: SO4
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-1,4-glucosidase	protein	471	44% helix, 16% strand	A3FPG4

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B
GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	782	0.76	0.80	50	empty
2	404	0.69	0.81	35	empty
3	386	0.68	0.80	37	GOL
4	382	0.67	0.80	38	GOL
5	88	0.47	0.82	22	empty

Interfaces

1 interface between chains.

A–B · 1642 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

5BWF · Crystal structure of the beta-glucosidase from Trichoderma harzianum · 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 A3FPG4
Elsewhere: RCSB PDB 5BWF · PDBe 5BWF · UniProt A3FPG4

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