Structure of PDB 4ysj Chain B

Receptor sequence
>4ysjB (length=462) Species: 5802 (Eimeria tenella) [Search protein sequence]
KLAATPGMFVQHSTAAFSDRYKGQRVLGKGSFGEVILCKDKVTGQEYAVK
VISKRLLKEVELLKKLDHPNIMKLYEFFEDKGYFYLVTEVYTGGELFDEI
ISRKRFSEVDAARIIRQVLSGITYMHKNKIVHRDLKPENLLLENKRKDAN
IRIIDFGLSTHFESTKKMKDKIGTAYYIAPEVLHGTYDEKCDVWSTGVIL
YILLSGCPPFNGANEFDILKKVEKGKFTFDLPQWKKVSEPAKDLIRKMLA
YVPTMRISARDALEHEWLKTTDADSIDVPSLESTILNIRQFQGTQKLAAA
ALLYMGSKLTTNEETVELNKIFQRMDKNGDGQLDKQELMEGYVELMKLKG
EDVSALDQSAIEFEVEQVLDAVDFDKNGFIEYSEFVTVAMDRKTLLSRQR
LERAFGMFDADGSGKISSSELATIFGVSEVDSETWRRVLAEVDRNNDGEV
DFEEFRQMLLKL
3D structure
PDB4ysj Potent and Selective Inhibitors of CDPK1 from T. gondii and C. parvum Based on a 5-Aminopyrazole-4-carboxamide Scaffold
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D151 K153 E155 N156 D172 T191
Catalytic site (residue number reindexed from 1) D134 K136 E138 N139 D155 T174
Enzyme Commision number ?
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004683 calcium/calmodulin-dependent protein kinase activity
GO:0005509 calcium ion binding
GO:0005516 calmodulin binding
GO:0005524 ATP binding
GO:0009931 calcium-dependent protein serine/threonine kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0035556 intracellular signal transduction
GO:0046777 protein autophosphorylation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4ysj, PDBe:4ysj, PDBj:4ysj
PDBsum4ysj
PubMed
UniProtQ3HNM4

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