MolNFT v1 · #63081 · protein

Crystal structure of putative alpha-L-fucosidase from bacteroides thetaiotaomicron

3EYP: “Crystal structure of putative alpha-L-fucosidase from bacteroides thetaiotaomicron”. X-ray diffraction, 7 pockets (best druggability 0.53). MolNFT v1 #63081 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3EYP
Type: protein
Length: 918 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative alpha-L-fucosidase
UniProt: Q8A5P6
Pockets: 7 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative alpha-L-fucosidase	protein	459	32% helix, 24% strand	Q8A5P6

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A, B

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	258	0.53	0.76	38	GOL
2	265	0.52	0.75	39	GOL
3	116	0.50	0.80	22	empty
4	66	0.47	0.83	17	GOL
5	139	0.42	0.75	28	empty

Interfaces

1 interface between chains.

A–B · 767 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3EYP · Crystal structure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron · 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 Q8A5P6
Elsewhere: RCSB PDB 3EYP · PDBe 3EYP · UniProt Q8A5P6

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