Research workbench
Crystal structure of human cellular retinol binding protein 2 (CRBP2) in complex with N-arachidonoylethanolamine (aea)
Analyse Crystal structure of human cellular retinol binding protein 2 (CRBP2) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BTI
- Type
- protein
- Length
- 273 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinol-binding protein 2
- UniProt
- P50120
- Ligands
- E7Y
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinol-binding protein 2 | protein | 136 | 10% helix, 54% strand | P50120 |
| B | Retinol-binding protein 2 | protein | 137 | 10% helix, 55% strand | P50120 |
Ligands and binding sites
- E7Y · (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide · ligand · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
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 | 315 | 0.85 | 0.94 | 41 | E7Y |
| 2 | 272 | 0.84 | 0.95 | 34 | E7Y |
| 3 | 140 | 0.47 | 0.78 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 588 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6BTI · Crystal structure of human cellular retinol binding protein 2 (CRBP2) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P50120 · AlphaFold monomer V2.0 prediction for retinol-binding protein 2 (P50120) · 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 P50120
- Elsewhere: RCSB PDB 6BTI · PDBe 6BTI · UniProt P50120
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