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Alpha-L-fucosidase complexed with inhibitor, pH-6FNJ

Analyse Alpha-L-fucosidase complexed with inhibitor, pH-6FNJ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZXB
Type: protein
Length: 884 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-L-fucosidase, putative
EC: 3.2.1.51
UniProt: Q9WYE2
Ligands: ZXB
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alpha-L-fucosidase, putative (EC 3.2.1.51)	protein	442	31% helix, 20% strand	Q9WYE2

Ligands and binding sites

ZXB · (2S,3R,4S,5R)-2-benzylpiperidine-3,4,5-triol · ligand · 2 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	964	0.72	0.76	61	empty
2	313	0.61	0.78	40	ZXB
3	315	0.60	0.78	44	ZXB
4	88	0.33	0.73	12	empty
5	94	0.33	0.72	13	empty

Interfaces

1 interface between chains.

A–B · 872 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2ZXB · alpha-L-fucosidase complexed with inhibitor, ph-6FNJ · 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 Q9WYE2
Elsewhere: RCSB PDB 2ZXB · PDBe 2ZXB · UniProt Q9WYE2

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