1V0O
Structure of P. falciparum PfPK5-Indirubin-5-sulphonate ligand complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0008353 | molecular_function | RNA polymerase II CTD heptapeptide repeat kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051301 | biological_process | cell division |
| A | 0051726 | biological_process | regulation of cell cycle |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0008353 | molecular_function | RNA polymerase II CTD heptapeptide repeat kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051301 | biological_process | cell division |
| B | 0051726 | biological_process | regulation of cell cycle |
| B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE INR A2638 |
| Chain | Residue |
| A | ILE10 |
| A | ASP85 |
| A | LEU132 |
| A | ASP143 |
| A | VAL18 |
| A | ALA30 |
| A | LYS32 |
| A | PHE79 |
| A | GLU80 |
| A | HIS81 |
| A | LEU82 |
| A | ASP83 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE INR B2638 |
| Chain | Residue |
| B | ILE10 |
| B | VAL18 |
| B | ALA30 |
| B | LYS32 |
| B | PHE79 |
| B | GLU80 |
| B | HIS81 |
| B | LEU82 |
| B | ASP83 |
| B | ASP85 |
| B | LEU132 |
| B | ASP143 |
| B | HOH2134 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 23 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkAqnnyget...........FALK |
| Chain | Residue | Details |
| A | ILE10-LYS32 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI |
| Chain | Residue | Details |
| A | VAL121-ILE133 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P24941","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P24941","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | GLN129 | |
| A | ASP125 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | GLN129 | |
| B | ASP125 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS127 | |
| A | ASP125 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS127 | |
| B | ASP125 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS127 | |
| A | ASP125 | |
| A | THR163 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS127 | |
| B | ASP125 | |
| B | THR163 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN130 | |
| A | LYS127 | |
| A | ASP125 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN130 | |
| B | LYS127 | |
| B | ASP125 |
