Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004689 | molecular_function | phosphorylase kinase activity |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005964 | cellular_component | phosphorylase kinase complex |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 382 |
| Chain | Residue |
| A | ASP167 |
| A | ATP381 |
| A | HOH446 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 383 |
| Chain | Residue |
| A | LYS151 |
| A | ASN154 |
| A | ASP167 |
| A | ATP381 |
| A | HOH403 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 381 |
| Chain | Residue |
| A | GLY26 |
| A | GLY28 |
| A | SER31 |
| A | VAL33 |
| A | ALA46 |
| A | LYS48 |
| A | ASP104 |
| A | MET106 |
| A | GLU110 |
| A | LYS124 |
| A | LYS151 |
| A | GLU153 |
| A | ASN154 |
| A | LEU156 |
| A | ASP167 |
| A | MN382 |
| A | MN383 |
| A | HOH402 |
| A | HOH403 |
| A | HOH411 |
| A | HOH446 |
| A | LEU25 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGVSSVVRrCihkptcke..........YAVK |
| Chain | Residue | Details |
| A | LEU25-LYS48 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILL |
| Chain | Residue | Details |
| A | ILE145-LEU157 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | LEU150 | |
| Chain | Residue | Details |
| A | GLY26 | |
| A | ILE49 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP149 | |
| A | GLU153 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS151 | |
| A | ASP149 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR186 | |
| A | LYS151 | |
| A | ASP149 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS151 | |
| A | ASN154 | |
| A | ASP149 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 35 |
| Chain | Residue | Details |
| A | ASP149 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS151 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN154 | metal ligand |
| A | ASP167 | metal ligand |
| A | THR186 | activator, hydrogen bond donor |
