Research workbench
Crystal structure of the mutant C2A conjugated bile acid hydrolase from clostridium perfringens
Analyse Crystal structure of the mutant C2A conjugated bile acid hydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RF8
- Type
- protein
- Length
- 657 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Choloylglycine hydrolase
- EC
- 3.5.1.24
- UniProt
- P54965
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Choloylglycine hydrolase (EC 3.5.1.24) | protein | 328 | 21% helix, 35% strand | P54965 |
| B | Choloylglycine hydrolase (EC 3.5.1.24) | protein | 329 | 18% helix, 34% strand | P54965 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.78 | 0.98 | 29 | empty |
| 2 | 396 | 0.69 | 0.81 | 46 | GOL |
| 3 | 407 | 0.68 | 0.80 | 47 | GOL |
| 4 | 105 | 0.36 | 0.74 | 25 | empty |
| 5 | 91 | 0.35 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3154 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 2RF8 · Crystal Structure of the mutant C2A conjugated bile acid hydrolase from Clostridium… · the same entry in another collection · chain A against A, TM-score 1.00
- P54965 · AlphaFold monomer V2.0 prediction for conjugated bile acid hydrolase (P54965) · a predicted model of the same protein · chain B 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 P54965
- Elsewhere: RCSB PDB 2RF8 · PDBe 2RF8 · UniProt P54965
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