MolNFT v1 · #17303 · protein
The crystal structures of holo-and apo-cellular retinol binding protein II
1OPA: “The crystal structures of holo-and apo-cellular retinol binding protein II”. X-ray diffraction, 3 pockets (best druggability 0.84). MolNFT v1 #17303 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OPA
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular retinol binding protein II
- UniProt
- P06768
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cellular retinol binding protein II | protein | 133 | 11% helix, 56% strand | P06768 |
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 | 303 | 0.84 | 0.95 | 34 | empty |
| 2 | 298 | 0.84 | 0.94 | 36 | empty |
| 3 | 103 | 0.37 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 390 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1OPA · The crystal structures of holo-and apo-cellular retinol binding protein II · the same entry in another collection · chain A against A, TM-score 1.00
- P06768 · AlphaFold monomer V2.0 prediction for retinol-binding protein 2 (P06768) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P06768
- Elsewhere: RCSB PDB 1OPA · PDBe 1OPA · UniProt P06768
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.