1DS5
DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.
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 | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0005956 | cellular_component | protein kinase CK2 complex |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009648 | biological_process | photoperiodism |
| A | 0010229 | biological_process | inflorescence development |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| 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 | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0005956 | cellular_component | protein kinase CK2 complex |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009648 | biological_process | photoperiodism |
| B | 0010229 | biological_process | inflorescence development |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0051726 | biological_process | regulation of cell cycle |
| B | 0106310 | molecular_function | protein serine kinase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005829 | cellular_component | cytosol |
| C | 0005956 | cellular_component | protein kinase CK2 complex |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0006974 | biological_process | DNA damage response |
| C | 0009648 | biological_process | photoperiodism |
| C | 0010229 | biological_process | inflorescence development |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0051726 | biological_process | regulation of cell cycle |
| C | 0106310 | molecular_function | protein serine kinase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005829 | cellular_component | cytosol |
| D | 0005956 | cellular_component | protein kinase CK2 complex |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0006974 | biological_process | DNA damage response |
| D | 0009648 | biological_process | photoperiodism |
| D | 0010229 | biological_process | inflorescence development |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0051726 | biological_process | regulation of cell cycle |
| D | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 1001 |
| Chain | Residue |
| D | HOH1059 |
| D | HOH1070 |
| D | HOH1071 |
| D | HOH1072 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 1002 |
| Chain | Residue |
| D | HOH1073 |
| D | HOH1074 |
| D | HOH1075 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1003 |
| Chain | Residue |
| B | ALA193 |
| B | HOH1073 |
| B | HOH1074 |
| B | HOH1075 |
| B | ARG191 |
| B | VAL192 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1004 |
| Chain | Residue |
| B | HOH1065 |
| B | HOH1076 |
| B | HOH1077 |
| B | HOH1078 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AMP A 501 |
| Chain | Residue |
| A | VAL45 |
| A | ILE66 |
| A | HIS160 |
| A | ASN161 |
| A | MET163 |
| A | ILE174 |
| A | ASP175 |
| B | ARG47 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP C 601 |
| Chain | Residue |
| C | VAL45 |
| C | GLY48 |
| C | VAL53 |
| C | ILE66 |
| C | VAL95 |
| C | GLU114 |
| C | VAL116 |
| C | ASN161 |
| C | MET163 |
| C | ILE174 |
| C | ASP175 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP D 701 |
| Chain | Residue |
| D | SER51 |
| D | VAL53 |
| D | ILE66 |
| D | LYS68 |
| D | GLU114 |
| D | VAL116 |
| D | ASN161 |
| D | MET163 |
| D | ASP175 |
| D | HOH1010 |
| D | HOH1053 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AMP B 801 |
| Chain | Residue |
| B | SER51 |
| B | VAL53 |
| B | ILE66 |
| B | LYS68 |
| B | GLU114 |
| B | VAL116 |
| B | HIS160 |
| B | MET163 |
| B | ILE174 |
| B | ASP175 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGKYSEVFeGinvnnnek..........CIIK |
| Chain | Residue | Details |
| A | VAL45-LYS68 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI |
| Chain | Residue | Details |
| A | ILE152-ILE164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | ASP156 | |
| B | ASP156 | |
| C | ASP156 | |
| D | ASP156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | VAL45 | |
| A | LYS68 | |
| B | VAL45 | |
| B | LYS68 | |
| C | VAL45 | |
| C | LYS68 | |
| D | VAL45 | |
| D | LYS68 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | HIS160 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | LYS158 | |
| B | SER194 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP156 | |
| C | LYS158 | |
| C | SER194 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP156 | |
| D | LYS158 | |
| D | SER194 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | ASN161 | |
| A | LYS158 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | ASN161 | |
| B | LYS158 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP156 | |
| C | ASN161 | |
| C | LYS158 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP156 | |
| D | ASN161 | |
| D | LYS158 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | HIS160 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP156 | |
| C | HIS160 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP156 | |
| D | HIS160 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | LYS158 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | LYS158 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP156 | |
| C | LYS158 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP156 | |
| D | LYS158 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | LYS158 | |
| A | SER194 |
