MolNFT v1 · #49463 · protein
Human EPHA3 kinase and juxtamembrane region, base, AMP-pnp bound structure
2QOQ · Ephrin receptor: “Human EPHA3 kinase and juxtamembrane region, base, AMP-pnp bound structure”. X-ray diffraction, 2 ligands (ANP, MG), 2 pockets (best druggability 0.59). MolNFT v1 #49463 on GenesisL1: 3D structure, binding sites…
- PDB
- 2QOQ
- Type
- protein
- Length
- 285 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
- Ligands
- ANP, MG
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin receptor (EC 2.7.10.1) | protein | 285 | 40% helix, 18% strand | Q6P4R6 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.59 | 0.78 | 37 | MG, ANP |
| 2 | 180 | 0.47 | 0.75 | 33 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 2QOQ · Human EphA3 kinase and juxtamembrane region, base, AMP-PNP bound 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 2QOQ · PDBe 2QOQ · UniProt Q6P4R6
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