Research workbench
Native structure of the extracellular domain of erythropoietin (epo) receptor [ebp]
Analyse Native structure of the extracellular domain of erythropoietin (epo) receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ERN
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (erythropoietin receptor)
- UniProt
- P19235
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (erythropoietin receptor) | protein | 207 | 9% helix, 44% strand | P19235 |
| B | Protein (erythropoietin receptor) | protein | 209 | 10% helix, 44% strand | P19235 |
Interfaces
1 interface between chains.
- A–B · 770 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1ERN · Native structure of the extracellular domain of erythropoietin (epo) receptor [ebp] · the same entry in another collection · chain A against A, TM-score 1.00
- P19235 · AlphaFold monomer V2.0 prediction for erythropoietin receptor (P19235) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P19235
- Elsewhere: RCSB PDB 1ERN · PDBe 1ERN · UniProt P19235
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