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Crystal structure of the EPHA2 intracellular kd-SAM domains

Analyse Crystal structure of the EPHA2 intracellular kd-SAM domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KJA
Type
protein
Length
713 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ephrin type-a receptor 2
EC
2.7.10.1
UniProt
P29317
Ligands
ACP, MG
Pockets
9 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEphrin type-a receptor 2 (EC 2.7.10.1)protein36445% helix, 13% strandP29317
BEphrin type-a receptor 2 (EC 2.7.10.1)protein34946% helix, 13% strandP29317

Ligands and binding sites

  • ACP · Phosphomethylphosphonic acid adenylate ester · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · chains A
  • GOL · Glycerol · additive · 5 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15930.680.7753GOL, ACP
22720.620.8030ACP, MG
32240.550.7836GOL
4990.430.7822empty
51020.390.7617empty

Interfaces

1 interface between chains.

  • A–B · 682 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7KJA · Crystal structure of the EphA2 intracellular KD-SAM domains · 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 B against A, TM-score 0.79

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