Research workbench
Crystal structure of ephrin A2 (EPHA2) receptor protein kinase with compound 2F
Analyse Crystal structure of ephrin A2 (EPHA2) receptor protein kinase with compound 2F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NK8
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29317
- Ligands
- 90Z
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 266 | — | P29317 |
Ligands and binding sites
- 90Z · ~{N}-(2-chloranyl-6-methyl-phenyl)-2-[[3-[(2,2,6,6-tetramethyl-1-oxidanyl-piperidin-4-yl) carbamoyl]phenyl]amino]-1,3-thiazole-5-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NK8 · Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 2f · the same entry in another collection · chain A against A, TM-score 1.00
- P29317 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 2 (P29317) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P29317
- Elsewhere: RCSB PDB 5NK8 · PDBe 5NK8 · UniProt P29317
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