Research workbench
Human EPHA3 kinase and juxtamembrane region bound to substrate KQWDNYE[PTYR]IW
Analyse Human EPHA3 kinase and juxtamembrane region bound to substrate KQWDNYE[PTYR]IW in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FXX
- Type
- protein
- Length
- 297 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-a receptor 3; Peptide substrate
- EC
- 2.7.10.1
- UniProt
- P29320
- Ligands
- ANP, MG
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-a receptor 3 (EC 2.7.10.1) | protein | 288 | 40% helix, 19% strand | P29320 |
| B | Peptide substrate | protein | 9 | 0% helix, 11% strand | — |
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
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 | 387 | 0.63 | 0.78 | 39 | MG, ANP |
Interfaces
1 interface between chains.
- A–B · 560 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3FXX · Human EphA3 Kinase and Juxtamembrane Region Bound to Substrate KQWDNYE[pTyr]IW · the same entry in another collection · chain A against A, TM-score 1.00
- P29320 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 3 (P29320) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 3FXX · PDBe 3FXX · UniProt P29320
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