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Complex structure of the GH93 alpha-L-arabinofuranosidase of fusarium graminearum with arabinobiose

Analyse Complex structure of the GH93 alpha-L-arabinofuranosidase of fusarium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W5O
Type: protein
Length: 359 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-L-arabinofuranosidase
EC: 3.2.1.55
Ligands: AHR, SO4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-L-arabinofuranosidase (EC 3.2.1.55)	protein	359	2% helix, 45% strand	—

Ligands and binding sites

AHR · alpha-L-arabinofuranose · sugar · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

2 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	467	0.70	0.80	31	empty
2	196	0.53	0.77	26	AHR

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2W5O · Complex structure of the GH93 alpha-L-arabinofuranosidase of Fusarium graminearum with… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2W5O · PDBe 2W5O

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