1EH2: EPS15

Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures. Determined by solution NMR. Released 22 Jul 1999.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
743
Mol. weight
11.98 kDa
Ligands
CA
Released
22 Jul 1999

Explore 1EH2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EH2 contains 4 α-helices and 2 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: 4 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix11-2111
β-strand3211
α-helix33-419
α-helix47-5711
β-strand6411
α-helix67-8216

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
EPS15Aprotein106Homo sapiensP42566 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1EH2_1 EPS15 (chains A)
NRWGSPWAVKPEDKAKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDID
HDGMLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWLEI

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1

Primary citation

Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. de Beer, T., Carter, R.E., Lobel-Rice, K.E. et al. Science (1998) 281:1357-1360. DOI 10.1126/science.281.5381.1357 · PubMed

Other PDB entries of the same protein (UniProt P42566 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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