1EDU: Enth domain of rat epsin 1

Crystal structure of the enth domain of rat epsin 1. Determined by X-ray diffraction at 1.8 Å resolution. Released 10 May 2000.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Rattus norvegicus
Chains
1
Atoms
1,289
Mol. weight
17.81 kDa
Released
10 May 2000

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

Secondary structure: helices and β-sheets

1EDU contains 12 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: 12 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix7-82
α-helix9-179
α-helix24-263
α-helix27-3610
α-helix40-5415
α-helix58-603
α-helix61-7717
α-helix80-889
α-helix90-945
α-helix95-984
β-strand10211
β-strand10811
α-helix110-12516
α-helix127-14519

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
EH domain binding protein EPSINAprotein149Rattus norvegicusO88339 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1EDU_1 EH domain binding protein EPSIN (chains A)
NIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNW
RHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLV
ALLRDEDRLREERAHALKTKEKLAQTATA

Primary citation

Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). Hyman, J., Chen, H., Di Fiore, P.P. et al. J Cell Biol (2000) 149:537-546. DOI 10.1083/jcb.149.3.537 · PubMed

Other PDB entries of the same protein (UniProt O88339 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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