3IIA: PDB entry 3IIA

Crystal structure of apo (91-244) RIa subunit of cAMP-dependent protein kinase. Determined by X-ray diffraction at 2.7 Å resolution. Released 11 Aug 2010.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Bos taurus
Chains
1
Atoms
1,071
Mol. weight
17.43 kDa
Released
11 Aug 2010

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

Secondary structure: helices and β-sheets

3IIA contains 7 α-helices and 10 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: 7 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix120-13011
α-helix142-1509
β-strand151-15661
β-strand16112
β-strand16513
β-strand16713
α-helix168-1692
β-strand171-17771
β-strand180-18452
β-strand187-19042
β-strand197-19821
α-helix201-2055
β-strand212-21542
β-strand219-22571
α-helix226-2294
α-helix230-2345
α-helix235-2417

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase type I-alpha regulatory subunitAprotein154Bos taurusP00514 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3IIA_1 cAMP-dependent protein kinase type I-alpha regulatory subunit (chains A)
GRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDA
MFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRA
ATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMY

Primary citation

Cyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design. Badireddy, S., Yunfeng, G., Ritchie, M. et al. Mol Cell Proteomics (2011) 10:M110.004390-M110.004390. DOI 10.1074/mcp.M110.004390 · PubMed

Other PDB entries of the same protein (UniProt P00514 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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