1FF1: Second EPS15 homology domain of human EPS15

Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfl. Determined by solution NMR. Released 1 Nov 2000.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
791
Mol. weight
11.71 kDa
Ligands
CA
Released
1 Nov 2000

Explore 1FF1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FF1 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-helix11-2111
β-strand3211
α-helix33-419
α-helix47-559
β-strand6411
α-helix67-8216
α-helix97-993

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Epidermal growth factor receptor substrate 15Aprotein95Homo sapiensP42566 (AlphaFold model)
Ptgssstnpfl peptideBprotein11
Sequence of entity 1 (A), FASTA
>1FF1_1 EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15 (chains A)
PWAVKPEDKAKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGML
DRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKR
Sequence of entity 2 (B), FASTA
>1FF1_2 PTGSSSTNPFL PEPTIDE (chains B)
PTGSSSTNPFL

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1

Primary citation

Molecular mechanism of NPF recognition by EH domains. de Beer, T., Hoofnagle, A.N., Enmon, J.L. et al. Nat Struct Biol (2000) 7:1018-1022. DOI 10.1038/80924 · PubMed

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

Browse structure collections

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