Research workbench
Crystal structure of recombinant chichen liver bile acid binding protein (cl-babp) in complex with cholic acid
Analyse Crystal structure of recombinant chichen liver bile acid binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O0K
- Type
- protein
- Length
- 251 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid-binding protein, liver
- UniProt
- P80226
- Ligands
- CHD
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid-binding protein, liver | protein | 125 | 11% helix, 57% strand | P80226 |
| B | Fatty acid-binding protein, liver | protein | 126 | 11% helix, 56% strand | P80226 |
Ligands and binding sites
- CHD · Cholic acid · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 739 | 0.85 | 0.87 | 44 | CHD |
| 2 | 732 | 0.84 | 0.86 | 47 | CHD |
| 3 | 155 | 0.41 | 0.73 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 262 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7O0K · Crystal structure of recombinant chichen liver Bile Acid Binding Protein (cL-BABP) in… · the same entry in another collection · chain A against A, TM-score 1.00
- P80226 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, liver (P80226) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P80226
- Elsewhere: RCSB PDB 7O0K · PDBe 7O0K · UniProt P80226
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