Structure of PDB 1szm Chain B Binding Site BS01

Receptor Information
>1szm Chain B (length=323) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHM
ETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDN
SNLYMVMEYAPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLI
YRDLKPENLMIDQQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSK
GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSS
DLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAP
FIPEEEEIRVSINEKCGKEFSEF
Ligand information
Ligand IDBI4
InChIInChI=1S/C27H26N4O2/c1-30-13-6-7-17(30)12-14-31-16-21(19-9-3-5-11-23(19)31)25-24(26(32)29-27(25)33)20-15-28-22-10-4-2-8-18(20)22/h2-5,8-11,15-17,28H,6-7,12-14H2,1H3,(H,29,32,33)/t17-/m0/s1
InChIKeyLBFDERUQORUFIN-KRWDZBQOSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CN1CCC[C@H]1CCn2cc(c3ccccc23)C4=C(C(=O)NC4=O)c5c[nH]c6ccccc56
OpenEye OEToolkits 1.5.0C[N@]1CCC[C@H]1CCn2cc(c3c2cccc3)C4=C(C(=O)NC4=O)c5c[nH]c6c5cccc6
ACDLabs 10.04O=C3C(c2c1ccccc1nc2)=C(C(=O)N3)c4c6ccccc6n(c4)CCC5N(C)CCC5
OpenEye OEToolkits 1.5.0CN1CCCC1CCn2cc(c3c2cccc3)C4=C(C(=O)NC4=O)c5c[nH]c6c5cccc6
CACTVS 3.341CN1CCC[CH]1CCn2cc(c3ccccc23)C4=C(C(=O)NC4=O)c5c[nH]c6ccccc56
FormulaC27 H26 N4 O2
Name3-(1H-INDOL-3-YL)-4-{1-[2-(1-METHYLPYRROLIDIN-2-YL)ETHYL]-1H-INDOL-3-YL}-1H-PYRROLE-2,5-DIONE
ChEMBL
DrugBankDB07458
ZINCZINC000003871740
PDB chain1szm Chain B Residue 351 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1szm The protein kinase C inhibitor bisindolyl maleimide 2 binds with reversed orientations to different conformations of protein kinase a.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		L49 T51 V57 A70 M120 Y122 A123 P124
Binding residue
(residue number reindexed from 1)		L36 T38 V44 A57 M107 Y109 A110 P111
Annotation score1
Binding affinityMOAD: ic50=2.94uM
Enzymatic activity
Catalytic site (original residue number in PDB) D166 K168 E170 N171 D184 T201
Catalytic site (residue number reindexed from 1) D153 K155 E157 N158 D171 T188
Enzyme Commision number 2.7.11.11: cAMP-dependent protein kinase.
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004679 AMP-activated protein kinase activity
GO:0004691 cAMP-dependent protein kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0019904 protein domain specific binding
GO:0034237 protein kinase A regulatory subunit binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0001707 mesoderm formation
GO:0006468 protein phosphorylation
GO:0010737 protein kinase A signaling
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0034605 cellular response to heat
GO:1904262 negative regulation of TORC1 signaling
Cellular Component
GO:0001669 acrosomal vesicle
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005952 cAMP-dependent protein kinase complex
GO:0031594 neuromuscular junction
GO:0036126 sperm flagellum
GO:0048471 perinuclear region of cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1szm, PDBe:1szm, PDBj:1szm
PDBsum1szm
PubMed14996846
UniProtP00517|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

[Back to BioLiP]