1C07: Third EPS15 homology domain of human EPS15

Structure of the third EPS15 homology domain of human EPS15. Determined by solution NMR. Released 19 Jul 2000.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
747
Mol. weight
10.67 kDa
Ligands
CA
Released
19 Jul 2000

Explore 1C07 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1C07 contains 5 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix15-2713
β-strand34-3521
α-helix37-459
α-helix51-6111
β-strand69-7021
α-helix74-8512
α-helix101-1022

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (epidermal growth factor receptor pathway substrate 15)Aprotein95Homo sapiensP42566 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1C07_1 PROTEIN (EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 15) (chains A)
TWVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGK
LSKDQFALAFHLISQKLIKGIDPPHVLTPEMIPPS

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1

Primary citation

Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites. Enmon, J.L., de Beer, T., Overduin, M. Biochemistry (2000) 39:4309-4319. DOI 10.1021/bi9927383 · 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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