Research workbench
Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 ångströms resolution
Analyse Crystal structure of the trigonal form of human plasma retinol-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BRQ
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinol binding protein
- UniProt
- P02753
- Pockets
- 1 · best druggability 0.84
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 | P02753 |
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 | 207 | 0.84 | 0.97 | 27 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1BRQ · Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5… · the same entry in another collection · chain A against A, TM-score 1.00
- P02753 · AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P02753) · 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 P02753
- Elsewhere: RCSB PDB 1BRQ · PDBe 1BRQ · UniProt P02753
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