Research workbench
B. theta bile salt hydrolase with covalent inhibitor
Analyse B. theta bile salt hydrolase with covalent inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UH4
- Type
- protein
- Length
- 1,293 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Choloylglycine hydrolase
- EC
- 3.5.1.24
- UniProt
- A0A0P0ENF5
- Ligands
- QC7
- Pockets
- 14 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 20% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Choloylglycine hydrolase (EC 3.5.1.24) | protein | 329 | 19% helix, 30% strand | A0A0P0ENF5 |
| B | Choloylglycine hydrolase (EC 3.5.1.24) | protein | 326 | 19% helix, 29% strand | A0A0P0ENF5 |
| C, D | Choloylglycine hydrolase (EC 3.5.1.24) | protein | 319 | 21% helix, 29% strand | A0A0P0ENF5 |
Ligands and binding sites
- QC7 · (5R,6R)-6-[(1S,2R,4aS,4bS,7R,8aS,10R,10aS)-7,10-dihydroxy-1,2,4b-trimethyltetradecahydrophenanthren-2-yl]-5-methylheptan-2-one · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 650 | 0.79 | 0.84 | 64 | QC7 |
| 2 | 516 | 0.79 | 0.86 | 38 | empty |
| 3 | 973 | 0.74 | 0.77 | 74 | empty |
| 4 | 369 | 0.70 | 0.82 | 36 | empty |
| 5 | 165 | 0.62 | 0.84 | 28 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1638 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 309 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 168 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 50 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6UH4 · B. theta Bile Salt Hydrolase with covalent inhibitor · 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 A0A0P0ENF5
- Elsewhere: RCSB PDB 6UH4 · PDBe 6UH4 · UniProt A0A0P0ENF5
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