MolNFT v1 · #166146 · protein
B. theta bile salt hydrolase with covalent inhibitor
6UH4: “B. theta bile salt hydrolase with covalent inhibitor”. X-ray diffraction, 1 ligand (QC7). MolNFT v1 #166146 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UH4
- Type
- protein
- Length
- 1,293 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0P0ENF5
- Ligands
- QC7
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 329 | — | A0A0P0ENF5 |
| B | — | protein | 326 | — | A0A0P0ENF5 |
| C, D | — | protein | 319 | — | 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.
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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