2P64: D domain of b-TrCP

D domain of b-TrCP. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Jun 2007.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
2
Atoms
890
Mol. weight
12.76 kDa
Ligands
CD
Released
19 Jun 2007

Explore 2P64 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2P64 contains 9 α-helices and 0 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: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix129-14113
α-helix146-15813
α-helix162-17211
α-helix173-1753
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix127-1293
α-helix130-14112
α-helix146-15813
α-helix162-17211
α-helix173-1764

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
F-box/WD repeat protein 1AA, Bprotein52Homo sapiensQ9Y297 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2P64_1 F-box/WD repeat protein 1A (chains A, B)
GAASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ

Ligands and cofactors

IDNameFormulaCopies
CDCadmium ionCd1

Primary citation

Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Tang, X., Orlicky, S., Lin, Z. et al. Cell (2007) 129:1165-1176. DOI 10.1016/j.cell.2007.04.042 · PubMed

Other PDB entries of the same protein (UniProt Q9Y297 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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