PPIRE15262

Target Protein Information
Protein_Name cGMP-dependent protein kinase 1
Protein_Sequence MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGKVNVTREDSPNEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF
Organism_Source Bos taurus
Functional_Classification serine threonine protein kinase
Cellular_Localization Cytoplasm
Gene_Names PRKG1
UniProt_ID P00516
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name [Ala33-Ala34]histone H2B(29-35)
Peptide_Sequence RKRSAAE
Peptide_Length 7
Peptide_SMILES C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 816.92
Aliphatic_Index 28.57143
Aromaticity 0.00000
Average_Rotatable_Bonds 4.14286
Charge_at_pH_7 1.99946
Isoelectric_Point 11.47970
Number_of_Hydrogen_Bond_Acceptors 13
Number_of_Hydrogen_Bond_Donors 17
Topological_Polar_Surface_Area 445.27000
X_logP_energy -6.14046
Interaction Information
Affinity KD=10.8 pM
Affinity_Assay fluorescence anisotropy titration
PDB_ID None
Type Substrate
Structure
Reference Information
Document_Type Research Articles
Title Synthetic peptide analogues differentially alter the binding affinities of cyclic nucleotide dependent protein kinases for nucleotide substrates
Release_Year 1988
PMID 2837278
DOI 10.1021/bi00406a027