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B. theta bile salt hydrolase

Analyse B. theta 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: 6UFY
Type: protein
Length: 1,307 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Choloylglycine hydrolase
UniProt: Q8A600
Pockets: 15 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 20% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Choloylglycine hydrolase	protein	326	20% helix, 31% strand	Q8A600
B	Choloylglycine hydrolase	protein	325	19% helix, 31% strand	Q8A600
D, C	Choloylglycine hydrolase	protein	328	20% helix, 31% strand	Q8A600

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	150	0.80	0.96	27	empty
2	134	0.80	0.97	29	empty
3	144	0.80	0.96	28	empty
4	139	0.79	0.96	31	empty
5	204	0.62	0.82	30	empty

Interfaces

6 interfaces between chains.

A–B · 1772 Å² buried · 26 hydrogen bonds · protein-protein
D–C · 1767 Å² buried · 23 hydrogen bonds · protein-protein
B–D · 597 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 557 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 226 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6UFY · B. theta Bile Salt Hydrolase · 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 Q8A600
Elsewhere: RCSB PDB 6UFY · PDBe 6UFY · UniProt Q8A600

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