4JVA: RIIbeta(108-402)

Crystal Structure of RIIbeta(108-402) bound to HE33, a N6 di-propyl substituted cAMP analog. Determined by X-ray diffraction at 2.5 Å resolution. Released 18 Sept 2013.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Rattus norvegicus
Chains
1
Atoms
2,143
Mol. weight
34.98 kDa
Ligands
1OR
Released
18 Sept 2013

Explore 4JVA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JVA contains 14 α-helices and 17 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: 14 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix137-14711
α-helix151-1533
α-helix158-16710
β-strand169-17351
β-strand178-18032
β-strand188-19471
β-strand196-20382
β-strand206-21492
β-strand218-21921
α-helix222-2265
β-strand233-23642
β-strand240-24671
α-helix247-2504
α-helix251-2555
α-helix256-26914
α-helix273-2753
α-helix282-2843
α-helix287-2893
β-strand291-29553
β-strand300-30233
β-strand310-31124
β-strand312-31325
β-strand314-323103
β-strand337-34263
β-strand347-34825
α-helix351-3544
β-strand362-373123
β-strand374-37524
α-helix376-3827
α-helix384-3863
α-helix387-3937

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase type II-beta regulatory subunitAprotein305Rattus norvegicusP12369 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4JVA_1 cAMP-dependent protein kinase type II-beta regulatory subunit (chains A)
SVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEK
LVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRA
ATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIG
TKVYNDGEQIIAQGDSADSFFIVESGEVRITMKRKGKSDIEENGAVEIARCLRGQYFGEL
ALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDI
VEPTA

Ligands and cofactors

IDNameFormulaCopies
1OR(2R,4aR,6R,7R,7aS)-6-[6-(dipropylamino)-9H-purin-9-yl]tetrahydro-4H-furo[3,2-d]…C16 H24 N5 O6 P2

Primary citation

Implementing Fluorescence Anisotropy Screening and Crystallographic Analysis to Define PKA Isoform-Selective Activation by cAMP Analogs. Brown, S.H., Cheng, C.Y., Saldanha, S.A. et al. ACS Chem Biol (2013) 8:2164-2172. DOI 10.1021/cb400247t · PubMed

Other PDB entries of the same protein (UniProt P12369 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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