3HBW: Fibroblast growth factor 13

Crystal Structure of Human Fibroblast Growth Factor Homologous Factor 2A (FHF2A), also referred to as Fibroblast Growth Factor 13A (FGF13A). Determined by X-ray diffraction at 1.9 Å resolution. Released 26 May 2009.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
2
Atoms
2,490
Mol. weight
43.69 kDa
Released
26 May 2009

Explore 3HBW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HBW contains 12 α-helices and 32 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: 6 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand66-75101
β-strand80-8341
β-strand89-9241
α-helix98-1003
β-strand102-10871
β-strand111-11661
α-helix1211
β-strand122-12541
β-strand131-13441
β-strand13712
α-helix139-1413
β-strand142-14871
β-strand152-161101
β-strand168-17031
β-strand17313
β-strand17811
β-strand17913
α-helix182-1843
α-helix190-1923
β-strand194-204111
α-helix205-2084
β-strand20912
Chain B: 6 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand1066-1075104
β-strand1080-108344
β-strand1089-109244
α-helix1098-11003
β-strand1102-110874
β-strand1111-111664
α-helix11211
β-strand1122-112544
β-strand1131-113444
β-strand113715
α-helix1139-11413
β-strand1142-114874
β-strand1152-1161104
β-strand1168-117034
β-strand117316
β-strand117814
β-strand117916
α-helix1182-11843
α-helix1190-11923
β-strand1194-1204114
α-helix1205-12084
β-strand120915

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Fibroblast growth factor 13A, Bprotein193Homo sapiensQ92913 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3HBW_1 Fibroblast growth factor 13 (chains A, B)
GSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVV
AIQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLG
LNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGV
LNGGKSMSHNEST

Primary citation

Crystal structure of a fibroblast growth factor homologous factor (FHF) defines a conserved surface on FHFs for binding and modulation of voltage-gated sodium channels. Goetz, R., Dover, K., Laezza, F. et al. J Biol Chem (2009) 284:17883-17896. DOI 10.1074/jbc.M109.001842 · PubMed

Other PDB entries of the same protein (UniProt Q92913 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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