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8EM8

Co-crystal structure of the cGMP-dependent protein kinase PKG from Plasmodium falciparum in complex with RY-1-165

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004691molecular_functioncAMP-dependent protein kinase activity
A0004692molecular_functioncGMP-dependent protein kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005952cellular_componentcAMP-dependent protein kinase complex
A0006468biological_processprotein phosphorylation
A0007276biological_processgamete generation
A0010737biological_processprotein kinase A signaling
A0016020cellular_componentmembrane
A0019898cellular_componentextrinsic component of membrane
A0030553molecular_functioncGMP binding
A0046872molecular_functionmetal ion binding
A0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGTFGTVKlVhhkptkir..........YALK
ChainResidueDetails
AILE547-LYS570

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL
ChainResidueDetails
AILE660-LEU672

site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIkQGEkGSyFFIInsG
ChainResidueDetails
AVAL85-GLY101
AILE203-GLY219
AILE445-GLY461

site_idPS00889
Number of Residues18
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEaALihntq......RSAtIiA
ChainResidueDetails
APHE121-ALA138
APHE239-ALA256
APHE481-SER498

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP664

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:31239348, ECO:0007744|PDB:5E16
ChainResidueDetails
ALYS113
AGLY122
AGLU123
AALA125
AARG132
ASER133

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25646845, ECO:0007744|PDB:4OFG
ChainResidueDetails
AARG473
AGLY482
AGLU483
AALA485
AARG492
ATHR493

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE547
ALYS570

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity => ECO:0000269|PubMed:25646845
ChainResidueDetails
AARG484
AGLN532
AASP533

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PDB entries from 2024-07-10

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