Research workbench
SAM domain of human ephrin type-a receptor 1 (EPHA1)
Analyse SAM domain of human ephrin type-a receptor 1 (EPHA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HIL
- Type
- protein
- Length
- 125 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-a receptor 1
- EC
- 2.7.10.1
- UniProt
- P21709
- Ligands
- CL, NO3
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-a receptor 1 (EC 2.7.10.1) | protein | 63 | 62% helix, 0% strand | P21709 |
| B | Ephrin type-a receptor 1 (EC 2.7.10.1) | protein | 62 | 61% helix, 0% strand | P21709 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 589 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 P21709
- Elsewhere: RCSB PDB 3HIL · PDBe 3HIL · UniProt P21709
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