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
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
A | 0004692 | molecular_function | cGMP-dependent protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007276 | biological_process | gamete generation |
A | 0010737 | biological_process | protein kinase A signaling |
A | 0016020 | cellular_component | membrane |
A | 0019898 | cellular_component | extrinsic component of membrane |
A | 0030553 | molecular_function | cGMP binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGTFGTVKlVhhkptkir..........YALK |
Chain | Residue | Details |
A | ILE547-LYS570 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL |
Chain | Residue | Details |
A | ILE660-LEU672 |
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIkQGEkGSyFFIInsG |
Chain | Residue | Details |
A | VAL85-GLY101 | |
A | ILE203-GLY219 | |
A | ILE445-GLY461 |
site_id | PS00889 |
Number of Residues | 18 |
Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEaALihntq......RSAtIiA |
Chain | Residue | Details |
A | PHE121-ALA138 | |
A | PHE239-ALA256 | |
A | PHE481-SER498 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ASP664 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31239348, ECO:0007744|PDB:5E16 |
Chain | Residue | Details |
A | LYS113 | |
A | GLY122 | |
A | GLU123 | |
A | ALA125 | |
A | ARG132 | |
A | SER133 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25646845, ECO:0007744|PDB:4OFG |
Chain | Residue | Details |
A | ARG473 | |
A | GLY482 | |
A | GLU483 | |
A | ALA485 | |
A | ARG492 | |
A | THR493 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ILE547 | |
A | LYS570 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | SITE: Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity => ECO:0000269|PubMed:25646845 |
Chain | Residue | Details |
A | ARG484 | |
A | GLN532 | |
A | ASP533 |