Research workbench

The crystal structure of native HYPBA1 from bifidobacterium longum jcm 1217

Analyse The crystal structure of native HYPBA1 from bifidobacterium longum jcm 1217 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WRE
Type: protein
Length: 634 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
Ligands: ZN
Pockets: 3 · 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	634	39% helix, 18% strand	E8MGH8

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

3 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	440	0.69	0.80	44	empty
2	337	0.60	0.77	37	empty
3	155	0.55	0.81	28	empty

Compared structures

3WRE · The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 · 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 3WRE · PDBe 3WRE · UniProt E8MGH8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.