1YWJ: FBP11WW1 domain

Structure of the FBP11WW1 domain. Determined by solution NMR. Released 12 Apr 2005.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 243
Mol. weight: 4.75 kDa
Released: 12 Apr 2005

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

Secondary structure: helices and β-sheets

1YWJ contains 1 α-helix and 3 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: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
β-strand	17-22	6	1
α-helix	23-25	3
β-strand	26-31	6	1
β-strand	36-38	3	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Formin-binding protein 3	A	protein	41	Homo sapiens	O75400 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1YWJ_1 Formin-binding protein 3 (chains A)
GSRRASVGSAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDD

Primary citation

Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain. Pires, J.R., Parthier, C., Aido-Machado, R. et al. J Mol Biol (2005) 348:399-408. DOI 10.1016/j.jmb.2005.02.056 · PubMed

Other PDB entries of the same protein (UniProt O75400 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1UZC The structure of an ff domain from human HYPA/FBP11
1YWI Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP
1ZR7 Solution structure of the first WW domain of FBP11
2CQN Solution structure of the FF domain of human Formin-binding protein 3
2DYF Solution structure of the first WW domain of FBP11 / HYPA (FBP11 WW1) complexed with a…
2KZG A Transient and Low Populated Protein Folding Intermediate at Atomic Resolution
2L5F Solution structure of the tandem WW domains from HYPA/FBP11
2L9V NMR structure of the FF domain L24A mutant's folding transition state
2LKS Ff11-60
8PXW Structure of the WW domain tandem of PRPF40A
8PXX Structure of the WW domain tandem of PRPF40A in complex with SF1

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