2Y7J
Structure of human phosphorylase kinase, gamma 2
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 |
| A | 0019865 | molecular_function | immunoglobulin binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004689 | molecular_function | phosphorylase kinase activity |
| B | 0005516 | molecular_function | calmodulin binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005964 | cellular_component | phosphorylase kinase complex |
| B | 0005977 | biological_process | glycogen metabolic process |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0019865 | molecular_function | immunoglobulin binding |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004689 | molecular_function | phosphorylase kinase activity |
| C | 0005516 | molecular_function | calmodulin binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005964 | cellular_component | phosphorylase kinase complex |
| C | 0005977 | biological_process | glycogen metabolic process |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0019865 | molecular_function | immunoglobulin binding |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004689 | molecular_function | phosphorylase kinase activity |
| D | 0005516 | molecular_function | calmodulin binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005964 | cellular_component | phosphorylase kinase complex |
| D | 0005977 | biological_process | glycogen metabolic process |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0019865 | molecular_function | immunoglobulin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE B49 A 1294 |
| Chain | Residue |
| A | VAL29 |
| A | GLY113 |
| A | LEU160 |
| A | ASP171 |
| A | HOH2063 |
| A | ILE30 |
| A | GLY31 |
| A | ARG32 |
| A | ALA51 |
| A | PHE107 |
| A | ASP108 |
| A | MET110 |
| A | ARG111 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE B49 B 1294 |
| Chain | Residue |
| B | VAL29 |
| B | ILE30 |
| B | ALA51 |
| B | ILE91 |
| B | PHE107 |
| B | ASP108 |
| B | MET110 |
| B | ARG111 |
| B | GLY113 |
| B | LEU160 |
| B | HOH2036 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE B49 C 1294 |
| Chain | Residue |
| C | ILE30 |
| C | ALA51 |
| C | ILE91 |
| C | PHE107 |
| C | ASP108 |
| C | MET110 |
| C | ARG111 |
| C | GLY113 |
| C | ASP117 |
| C | LEU160 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE B49 D 1294 |
| Chain | Residue |
| D | ILE30 |
| D | ALA51 |
| D | PHE107 |
| D | ASP108 |
| D | LEU109 |
| D | MET110 |
| D | ARG111 |
| D | GLY113 |
| D | LEU160 |
| D | HOH2028 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGVSSVVRrCvhratghe..........FAVK |
| Chain | Residue | Details |
| A | ILE30-LYS53 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILL |
| Chain | Residue | Details |
| A | ILE149-LEU161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP153 | |
| B | ASP153 | |
| C | ASP153 | |
| D | ASP153 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE30 | |
| A | LYS53 | |
| B | ILE30 | |
| B | LYS53 | |
| C | ILE30 | |
| C | LYS53 | |
| D | ILE30 | |
| D | LYS53 |
