Research workbench
Human EPHA3 kinase domain in complex with quinoxaline derivatives
Analyse Human EPHA3 kinase domain in complex with quinoxaline derivatives in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P4C
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eph receptor A3
- EC
- 2.7.10.1
- UniProt
- Q6P4R6
- Ligands
- 25Q
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eph receptor A3 (EC 2.7.10.1) | protein | 266 | 42% helix, 19% strand | Q6P4R6 |
Ligands and binding sites
- 25Q · 2-amino-1-(3-methoxyphenyl)-1H-pyrrolo[2,3-b]quinoxaline-3-carboxamide · ligand · 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 | 240 | 0.59 | 0.79 | 27 | 25Q |
| 2 | 50 | 0.27 | 0.74 | 14 | empty |
Compared structures
- 4P4C · Human EphA3 Kinase domain in complex with quinoxaline derivatives · 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 4P4C · PDBe 4P4C · UniProt Q6P4R6
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