1HYJ: EEA1 fyve domain

Solution structure of the EEA1 fyve domain. Determined by solution NMR. Released 14 Mar 2001.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 501
Mol. weight: 7.36 kDa
Ligands: ZN
Released: 14 Mar 2001

Explore 1HYJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HYJ contains 2 α-helices and 4 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	26-27	2	1
β-strand	34-35	2	1
β-strand	43-46	4	2
β-strand	49-54	6	2
α-helix	57-63	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endosome-associated protein	A	protein	65	Homo sapiens	Q15075 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1HYJ_1 ENDOSOME-ASSOCIATED PROTEIN (chains A)
RKWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACF
NDLQG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Structural mechanism of endosome docking by the FYVE domain. Kutateladze, T., Overduin, M. Science (2001) 291:1793-1796. DOI 10.1126/science.291.5509.1793 · PubMed

Other PDB entries of the same protein (UniProt Q15075 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3MJH 2.03 Å, Crystal Structure of Human Rab5A in complex with the C2H2 Zinc Finger of EEA1
1JOC 2.2 Å, EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate
1HYI Solution structure of the EEA1 fyve domain complexed with inositol 1,3-bisphosphate

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