2BUJ
Crystal structure of the human Serine-threonine Kinase 16 in complex with staurosporine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005798 | cellular_component | Golgi-associated vesicle |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006468 | biological_process | protein phosphorylation |
A | 0016020 | cellular_component | membrane |
A | 0016310 | biological_process | phosphorylation |
A | 0044024 | molecular_function | histone H2AS1 kinase activity |
A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
A | 0046777 | biological_process | protein autophosphorylation |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0071560 | biological_process | cellular response to transforming growth factor beta stimulus |
A | 0106310 | molecular_function | protein serine kinase activity |
B | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005798 | cellular_component | Golgi-associated vesicle |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006338 | biological_process | chromatin remodeling |
B | 0006468 | biological_process | protein phosphorylation |
B | 0016020 | cellular_component | membrane |
B | 0016310 | biological_process | phosphorylation |
B | 0044024 | molecular_function | histone H2AS1 kinase activity |
B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
B | 0046777 | biological_process | protein autophosphorylation |
B | 0048471 | cellular_component | perinuclear region of cytoplasm |
B | 0071560 | biological_process | cellular response to transforming growth factor beta stimulus |
B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A1300 |
Chain | Residue |
A | ARG59 |
A | STU1302 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B1298 |
Chain | Residue |
B | GLY30 |
B | SER32 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE STU A1301 |
Chain | Residue |
A | PHE100 |
A | PHE101 |
A | MET165 |
A | LEU26 |
A | GLU28 |
A | VAL34 |
A | ALA47 |
A | PRO99 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE STU A1302 |
Chain | Residue |
A | GLU87 |
A | HIS92 |
A | CL1300 |
B | GLN24 |
B | STU1300 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE STU B1299 |
Chain | Residue |
B | LEU26 |
B | GLY27 |
B | GLU28 |
B | ALA47 |
B | PRO99 |
B | PHE100 |
B | PHE101 |
B | MET165 |
B | STU1300 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE STU B1300 |
Chain | Residue |
A | HIS54 |
A | GLU55 |
A | STU1302 |
B | GLN24 |
B | LEU26 |
B | PHE45 |
B | PHE100 |
B | LYS102 |
B | ARG103 |
B | GLY104 |
B | STU1299 |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKptNILL |
Chain | Residue | Details |
A | TYR144-LEU156 |
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 | LEU149 | |
B | LEU149 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | GLY27 | |
A | ARG50 | |
B | GLY27 | |
B | ARG50 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:18184589 |
Chain | Residue | Details |
A | LEU186 | |
B | LEU186 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18184589 |
Chain | Residue | Details |
A | TYR198 | |
B | TYR198 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18184589 |
Chain | Residue | Details |
A | ARG199 | |
B | ARG199 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR152 | |
A | ASP148 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR152 | |
B | ASP148 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP148 | |
A | LYS150 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP148 | |
B | LYS150 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR195 | |
A | ASP148 | |
A | LYS150 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR195 | |
B | ASP148 | |
B | LYS150 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP148 | |
A | LYS150 | |
A | ASN153 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP148 | |
B | LYS150 | |
B | ASN153 |