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Crystal structure of thermotoga maritima alpha-fucosidase

Analyse Crystal structure of thermotoga maritima alpha-fucosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HL8
Type: protein
Length: 848 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.4
Source: THERMOTOGA MARITIMA
Molecule: Putative alpha-L-fucosidase
EC: 3.2.1.51
UniProt: Q9WYE2
Pockets: 4 · best druggability 0.53

Structure

x-ray diffraction · resolution 2.4 · 2 distinct chains · 32% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative alpha-L-fucosidase (EC 3.2.1.51)	protein	426	32% helix, 20% strand	Q9WYE2
B	Putative alpha-L-fucosidase (EC 3.2.1.51)	protein	422	32% helix, 19% strand	Q9WYE2

Pockets

4 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	181	0.53	0.78	21	empty
2	135	0.51	0.79	19	empty
3	66	0.30	0.74	15	empty
4	51	0.26	0.73	11	empty

Modifications

Observed in the structure: 2 disulfide, 2 modified (disulfide, carboxylation).

Compared structures

1HL8 · Crystal structure of thermotoga maritima alpha-fucosidase · 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 1HL8 · PDBe 1HL8 · UniProt Q9WYE2

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