2HO2: Human FE65-WW domain

Structure of human FE65-WW domain in complex with hMena peptide. Determined by X-ray diffraction at 1.33 Å resolution. Released 10 Jul 2007.

Method
X-ray diffraction
Resolution
1.33 Å
Organism
Homo sapiens
Chains
2
Atoms
389
Mol. weight
5.29 kDa
Released
10 Jul 2007

Explore 2HO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HO2 contains 1 α-helix and 3 β-strands across 2 chains. 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: 0 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand259-26351
β-strand268-27251
β-strand277-27931
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-98

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Amyloid beta A4 protein-binding family B member 1Aprotein38Homo sapiensO00213 (AlphaFold model)
Protein enabled homologBprotein10Q8N8S7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2HO2_1 Amyloid beta A4 protein-binding family B member 1 (chains A)
GSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPS
Sequence of entity 2 (B), FASTA
>2HO2_2 Protein enabled homolog (chains B)
PPPPPPPPPL

Primary citation

Structural Basis for Polyproline Recognition by the FE65 WW Domain. Meiyappan, M., Birrane, G., Ladias, J.A. J Mol Biol (2007) 372:970-980. DOI 10.1016/j.jmb.2007.06.064 · PubMed

Other PDB entries of the same protein (UniProt O00213 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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