MolNFT v1 · #16946 · protein

Crystal structure of thermotoga maritima alpha-fucosidase in complex with fucose

1ODU · Putative alpha-L-fucosidase: “Crystal structure of thermotoga maritima alpha-fucosidase in complex with fucose”. X-ray diffraction, 1 ligand (FUL), 7 pockets (best druggability 0.50). MolNFT v1 #16946 on GenesisL1: 3D structure…

PDB: 1ODU
Type: protein
Length: 846 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative alpha-L-fucosidase
EC: 3.2.1.51
UniProt: Q9WYE2
Ligands: FUL
Pockets: 7 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative alpha-L-fucosidase (EC 3.2.1.51)	protein	422	32% helix, 20% strand	Q9WYE2
B	Putative alpha-L-fucosidase (EC 3.2.1.51)	protein	424	33% helix, 20% strand	Q9WYE2

Ligands and binding sites

FUL · beta-L-fucopyranose · sugar · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	108	0.50	0.80	20	FUL
2	97	0.47	0.80	19	FUL
3	61	0.33	0.77	17	empty
4	64	0.31	0.75	12	empty
5	75	0.31	0.74	21	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1ODU · Crystal structure of thermotoga maritima alpha-fucosidase in complex with fucose · 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 1ODU · PDBe 1ODU · UniProt Q9WYE2

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