MolNFT v1 · #12432 · protein
Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol
1KGL · Cellular retinol-binding protein type I: “Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol”. Solution nmr, 1 ligand (RTL), 1 pocket (best druggability 0.80). MolNFT v1 #12432 on…
- PDB
- 1KGL
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular retinol-binding protein type I
- UniProt
- P02696
- Ligands
- RTL
- Pockets
- 1 · best druggability 0.80
Structure
solution nmr · 1 distinct chain · 12% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular retinol-binding protein type I | protein | 135 | 12% helix, 55% strand | P02696 |
Ligands and binding sites
- RTL · Retinol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.80 | 0.92 | 32 | RTL |
Compared structures
- 1KGL · Solution structure of cellular retinol binding protein type-I in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P02696 · AlphaFold monomer V2.0 prediction for retinol-binding protein 1 (P02696) · 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 P02696
- Elsewhere: RCSB PDB 1KGL · PDBe 1KGL · UniProt P02696
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.