Research workbench
Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein
Analyse Crystal structure of liganded and unliganded forms of bovine plasma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HBP
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinol binding protein
- UniProt
- P18902
- Ligands
- RTL
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinol binding protein | protein | 174 | 11% helix, 47% strand | P18902 |
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 | 232 | 0.82 | 0.94 | 30 | RTL |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1HBP · Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding… · the same entry in another collection · chain A against A, TM-score 1.00
- P18902 · AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P18902) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P18902
- Elsewhere: RCSB PDB 1HBP · PDBe 1HBP · UniProt P18902
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