1V0P
Structure of P. falciparum PfPK5-Purvalanol B ligand complex
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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 14 |
Details | BINDING SITE FOR RESIDUE PVB A 1287 |
Chain | Residue |
A | ILE10 |
A | GLN129 |
A | LEU132 |
A | ALA142 |
A | HOH2144 |
A | HOH2145 |
A | GLY11 |
A | GLU12 |
A | GLY13 |
A | ALA30 |
A | GLU80 |
A | LEU82 |
A | ASP83 |
A | ASP85 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PVB B 1287 |
Chain | Residue |
B | ILE10 |
B | GLY11 |
B | GLU12 |
B | GLY13 |
B | ALA30 |
B | PHE79 |
B | GLU80 |
B | HIS81 |
B | LEU82 |
B | ASP83 |
B | ASP85 |
B | GLN129 |
B | LEU132 |
B | ALA142 |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP125 | |
B | ASP125 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ILE10 | |
A | LYS32 | |
B | ILE10 | |
B | LYS32 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P24941 |
Chain | Residue | Details |
A | THR14 | |
A | THR158 | |
B | THR14 | |
B | THR158 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P24941 |
Chain | Residue | Details |
A | TYR15 | |
B | TYR15 |
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 |
A | ASN130 | |
A | LYS127 | |
A | ASP125 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN130 | |
B | LYS127 | |
B | ASP125 |