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Crystal structure of GH127 beta-L-arabinofuranosidase HYPBA1 from bifidobacterium longum ligand free form

Analyse Crystal structure of GH127 beta-L-arabinofuranosidase HYPBA1 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WKW
Type: protein
Length: 638 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-reducing end beta-L-arabinofuranosidase
EC: 3.2.1.185
UniProt: E8MGH8
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-reducing end beta-L-arabinofuranosidase (EC 3.2.1.185)	protein	638	39% helix, 18% strand	E8MGH8

Pockets

4 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	630	0.69	0.77	56	empty
2	371	0.67	0.81	35	empty
3	323	0.60	0.77	35	empty
4	52	0.39	0.81	15	empty

Compared structures

3WKW · Crystal structure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum… · the same entry in another collection · chain A against A, TM-score 1.00
E8MGH8 · AlphaFold monomer V2.0 prediction for non-reducing end beta-L- arabinofuranosidase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 E8MGH8
Elsewhere: RCSB PDB 3WKW · PDBe 3WKW · UniProt E8MGH8

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