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Bifidobacterium longum bile salt hydrolase

Analyse Bifidobacterium longum bile salt hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HF0
Type: protein
Length: 632 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile salt hydrolase
EC: 3.5.1.24
UniProt: Q9KK62
Pockets: 8 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bile salt hydrolase (EC 3.5.1.24)	protein	316	17% helix, 33% strand	Q9KK62

Pockets

8 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	250	0.80	0.93	41	empty
2	504	0.73	0.82	53	empty
3	404	0.63	0.77	36	empty
4	89	0.49	0.82	22	empty
5	162	0.46	0.76	22	empty

Interfaces

1 interface between chains.

A–B · 2021 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

2HF0 · Bifidobacterium longum bile salt hydrolase · the same entry in another collection · chain A against A, TM-score 1.00
Q9KK62 · AlphaFold monomer V2.0 prediction for conjugated bile acid hydrolase (Q9KK62) · a predicted model of the same protein · chain B 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 Q9KK62
Elsewhere: RCSB PDB 2HF0 · PDBe 2HF0 · UniProt Q9KK62

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