1FHR: FHA2 domain of RAD53

Solution structure of the FHA2 domain of RAD53 complexed with a phosphotyrosyl peptide. Determined by solution NMR. Released 18 Oct 2000.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
1,344
Mol. weight
19.16 kDa
Released
18 Oct 2000

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

Secondary structure: helices and β-sheets

1FHR contains 2 α-helices and 13 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: 2 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand578-58251
β-strand592-59431
β-strand601-60442
β-strand611-61222
β-strand623-63082
α-helix631-6322
β-strand644-65182
β-strand657-65931
β-strand662-66431
β-strand668-67142
β-strand676-68381
β-strand688-69691
β-strand70212
β-strand717-71822
α-helix721-7266

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein kinase SPK1Aprotein158Saccharomyces cerevisiaeP22216 (AlphaFold model)
DNA repair protein RAD9Pprotein7P14737 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1FHR_1 PROTEIN KINASE SPK1 (chains A)
GNGRFLTLKPLPDSIIQESLEIQQGVNPFFIGRSEDCNCKIEDNRLSRVHCFIFKKRHAV
GKSMYESPAQGLDDIWYCHTGTNVSYLNNNRMIQGTKFLLQDGDEIKIIWDKNNKFVIGF
KVEINDTTGLFNEGLGMLQEQRVVLKQTAEEKDLVKKL
Sequence of entity 2 (P), FASTA
>1FHR_2 DNA REPAIR PROTEIN RAD9 (chains P)
EDIYYLD

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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