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Crystal structure of rat alpha 1-macroglobulin receptor binding domain
Analyse Crystal structure of rat alpha 1-macroglobulin receptor binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EDY
- Type
- protein
- Length
- 264 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha 1-macroglobulin
- UniProt
- Q63332
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha 1-macroglobulin | protein | 134 | 7% helix, 48% strand | Q63332 |
| B | Alpha 1-macroglobulin | protein | 130 | 7% helix, 50% strand | Q63332 |
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 | 53 | 0.31 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 680 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1EDY · Crystal structure of rat alpha 1-macroglobulin receptor binding domain · the same entry in another collection · chain A against A, TM-score 1.00
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 Q63332
- Elsewhere: RCSB PDB 1EDY · PDBe 1EDY · UniProt Q63332
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