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SAM domain of human ephrin type-a receptor 1 (EPHA1)

Analyse SAM domain of human ephrin type-a receptor 1 (EPHA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HIL
Type
protein
Length
125 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ephrin type-a receptor 1
EC
2.7.10.1
UniProt
P21709
Ligands
CL, NO3

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEphrin type-a receptor 1 (EC 2.7.10.1)protein6362% helix, 0% strandP21709
BEphrin type-a receptor 1 (EC 2.7.10.1)protein6261% helix, 0% strandP21709

Ligands and binding sites

  • CL · Chloride ion · ion · chains A
  • NO3 · Nitrate ion · ion · chains A

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

Interfaces

1 interface between chains.

  • A–B · 589 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 3HIL · SAM Domain of Human Ephrin Type-A Receptor 1 (EphA1) · the same entry in another collection · chain A against A, TM-score 1.00
  • P21709 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 1 (P21709) · a predicted model of the same protein · chain B against A, TM-score 0.96

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