Structure of PDB 4yga Chain G

Receptor sequence
>4ygaG (length=447) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
AIFSDRYKGQRVLGKGSFGEVILCKDKITGQECAVKVISKRQVKQKTDKE
SLLREVQLLKQLDHPNIMKLYEFFEDKGYFYLVGEVYTGGELFDEIISRK
RFSEVDAARIIRQVLSGITYMHKNKIVHRDLKPENLLLESKSKDANIRII
DFGLSTHFEASKKIGTAYYIAPEVLHGTYDEKCDVWSTGVILYILLSGCP
PFNGANEYDILKKVEKGKYTFELPQWKKVSESAKDLIRKMLTYVPSMRIS
ARDALDHEWIQTYTKVPSLDNAILNIRQFQGTQKLAQAALLYMGSKLTSQ
DETKELTAIFHKMDKNGDGQLDRAELIEGYKELMRMKDASMLDASAVEHE
VDQVLDAVDFDKNGYIEYSEFVTVAMDRKTLLSRERLERAFRMFDSDNSG
KISSTELATIFGVSDVETWKSVLSEVDKNNDGEVDFDEFQQMLLKLC
3D structure
PDB4yga Allosteric activation of apicomplexan calcium-dependent protein kinases.
ChainG
Resolution2.94 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D174 K176 E178 N179 D195 T214
Catalytic site (residue number reindexed from 1) D130 K132 E134 N135 D151 T166
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA G D368 N370 D372 Q374 E379 D314 N316 D318 Q320 E325
BS02 CA G D415 D417 N419 Y421 E423 E426 D359 D361 N363 Y365 E367 E370
BS03 CA G D451 D453 S455 K457 E462 D395 D397 S399 K401 E406
BS04 CA G D485 N487 D489 E491 D493 E496 D427 N429 D431 E433 D435 E438
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4yga, PDBe:4yga, PDBj:4yga
PDBsum4yga
PubMed26305940
UniProtQ9BJF5

[Back to BioLiP]