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Crystal structure of the ligand-binding domain of the EPHB2 receptor tyrosine kinase

Analyse Crystal structure of the ligand-binding domain of the EPHB2 receptor tyrosine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NUK
Type
protein
Length
169 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (tyrosine-protein kinase receptor eph)
EC
2.7.1.112
UniProt
P54763
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (tyrosine-protein kinase receptor eph) (EC 2.7.1.112)protein1692% helix, 40% strandP54763

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.310.7614empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1NUK · Crystal structure of the ligand-binding domain of the EPHB2 receptor tyrosine kinase · the same entry in another collection · chain A against A, TM-score 1.00
  • P54763 · AlphaFold monomer V2.0 prediction for ephrin type-B receptor 2 (P54763) · a predicted model of the same protein · chain A against A, TM-score 0.93

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