Research workbench
Ensemble of the solution structures of domain one of receptor associated protein
Analyse Ensemble of the solution structures of domain one of receptor associated protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OV2
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-2-macroglobulin receptor-associated protein precursor
- UniProt
- P30533
- Pockets
- 1 · best druggability 0.28
Structure
solution nmr · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-2-macroglobulin receptor-associated protein precursor | protein | 82 | 70% helix, 0% strand | P30533 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.28 | 0.73 | 13 | empty |
Compared structures
- 1OV2 · Ensemble of the solution structures of domain one of receptor associated protein · the same entry in another collection · chain A against A, TM-score 1.00
- P30533 · AlphaFold monomer V2.0 prediction for alpha-2-macroglobulin receptor- associated protein… · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P30533
- Elsewhere: RCSB PDB 1OV2 · PDBe 1OV2 · UniProt P30533
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