2HWN: RII alpha Dimerization/Docking domain of PKA

Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide. Determined by X-ray diffraction at 1.6 Å resolution. Released 21 Nov 2006.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Rattus norvegicus
Chains
6
Atoms
1,853
Mol. weight
26.47 kDa
Released
21 Nov 2006

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

Secondary structure: helices and β-sheets

2HWN contains 11 α-helices and 0 β-strands across 6 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.

Chains A and D: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-2315
α-helix28-4215
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix9-2315
α-helix28-4316
Chain C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-62
α-helix9-2315
α-helix28-4215
Chain E: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1916
Chain F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-2017

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase type II-alpha regulatory subunitA, B, C, Dprotein45Rattus norvegicusP12368 (AlphaFold model)
A Kinase binding peptideE, Fprotein22Q4R5S0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2HWN_1 cAMP-dependent protein kinase type II-alpha regulatory subunit (chains A, B, C, D)
MSHIQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREARR
Sequence of entity 2 (E, F), FASTA
>2HWN_2 A Kinase binding peptide (chains E, F)
QEELAWKIAKMIVSDVMQQCKK

Primary citation

A Dynamic Mechanism for AKAP Binding to RII Isoforms of cAMP-Dependent Protein Kinase. Kinderman, F.S., Kim, C., von Daake, S. et al. Mol Cell (2006) 24:397-408. DOI 10.1016/j.molcel.2006.09.015 · PubMed

Other PDB entries of the same protein (UniProt P12368 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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