MolNFT v1 · #106999 · protein
Human EPHA3 kinase domain in complex with compound 164
4TWO · Ephrin type-a receptor 3: “Human EPHA3 kinase domain in complex with compound 164”. X-ray diffraction, 1 ligand (37W), 1 pocket (best druggability 0.63). MolNFT v1 #106999 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4TWO
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-a receptor 3
- EC
- 2.7.10.1
- UniProt
- P29320
- Ligands
- 37W
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-a receptor 3 (EC 2.7.10.1) | protein | 278 | 39% helix, 19% strand | P29320 |
Ligands and binding sites
- 37W · 5-{[3-carbamoyl-4-(3,4-dimethylphenyl)-5-methylthiophen-2-yl]amino}-5-oxopentanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.63 | 0.80 | 40 | 37W |
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 P29320
- Elsewhere: RCSB PDB 4TWO · PDBe 4TWO · UniProt P29320
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