Research workbench
Human EPHA3 kinase and juxtamembrane region, dephosphorylated, apo structure
Analyse Human EPHA3 kinase and juxtamembrane region, dephosphorylated, apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QO2
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin receptor
- EC
- 2.7.10.1
- UniProt
- Q6P4R6
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin receptor (EC 2.7.10.1) | protein | 282 | 41% helix, 18% strand | Q6P4R6 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.56 | 0.76 | 35 | empty |
| 2 | 103 | 0.39 | 0.76 | 25 | empty |
| 3 | 52 | 0.28 | 0.74 | 20 | empty |
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 2QO2 · Human EphA3 kinase and juxtamembrane region, dephosphorylated, apo structure · 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 Q6P4R6
- Elsewhere: RCSB PDB 2QO2 · PDBe 2QO2 · UniProt Q6P4R6
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