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Crystal structure of RBP4 bound to oleic acid
Analyse Crystal structure of RBP4 bound to oleic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WQ9
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinol-binding protein 4
- UniProt
- P02753
- Ligands
- OLA, CL
- Pockets
- 2 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinol-binding protein 4 | protein | 173 | 12% helix, 47% strand | P02753 |
Ligands and binding sites
- OLA · Oleic acid · ligand · chains A
- CL · Chloride ion · ion · 5 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.84 | 0.98 | 27 | OLA |
| 2 | 67 | 0.31 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 P02753
- Elsewhere: RCSB PDB 2WQ9 · PDBe 2WQ9 · UniProt P02753
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