1FHQ: FHA2 domain of RAD53

Refined solution structure of the FHA2 domain of RAD53. Determined by solution NMR. Released 18 Oct 2000.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
1,274
Mol. weight
18.15 kDa
Released
18 Oct 2000

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

Secondary structure: helices and β-sheets

1FHQ contains 3 α-helices and 15 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: 3 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand576-58271
β-strand592-59541
β-strand601-60442
β-strand611-61222
β-strand623-62972
β-strand645-65172
β-strand657-65931
β-strand662-66431
β-strand668-67142
β-strand676-67941
β-strand68213
β-strand68913
β-strand692-69651
β-strand70212
α-helix7161
β-strand717-71822
α-helix7191
α-helix721-7299

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein kinase SPK1Aprotein158Saccharomyces cerevisiaeP22216 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1FHQ_1 PROTEIN KINASE SPK1 (chains A)
GNGRFLTLKPLPDSIIQESLEIQQGVNPFFIGRSEDCNCKIEDNRLSRVHCFIFKKRHAV
GKSMYESPAQGLDDIWYCHTGTNVSYLNNNRMIQGTKFLLQDGDEIKIIWDKNNKFVIGF
KVEINDTTGLFNEGLGMLQEQRVVLKQTAEEKDLVKKL

Primary citation

II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides. Wang, P., Byeon, I.J., Liao, H. et al. J Mol Biol (2000) 302:927-940. DOI 10.1006/jmbi.2000.4095 · PubMed

Other PDB entries of the same protein (UniProt P22216 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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