Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1501 |
| Chain | Residue |
| A | ASN368 |
| A | ASP381 |
| A | HOH1512 |
| A | HOH1525 |
| E | 1121101 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1601 |
| Chain | Residue |
| F | 1121201 |
| B | ASN368 |
| B | ASP381 |
| F | HOH268 |
| F | HOH269 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1701 |
| Chain | Residue |
| C | ASN368 |
| C | ASP381 |
| C | HOH1795 |
| G | HOH7 |
| G | 1121301 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1801 |
| Chain | Residue |
| D | ASN368 |
| D | ASP381 |
| D | HOH1928 |
| H | 1121401 |
| H | HOH1402 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 112 E 1101 |
| Chain | Residue |
| A | LEU248 |
| A | GLY250 |
| A | GLY251 |
| A | GLN252 |
| A | TYR253 |
| A | GLY254 |
| A | VAL256 |
| A | ALA269 |
| A | LYS271 |
| A | THR315 |
| A | GLU316 |
| A | MET318 |
| A | ASN322 |
| A | ARG367 |
| A | ASN368 |
| A | LEU370 |
| A | ASP381 |
| A | MG1501 |
| A | HOH1512 |
| A | HOH1525 |
| A | HOH1541 |
| A | HOH1560 |
| E | PHE107 |
| E | HOH1103 |
| E | HOH1104 |
| E | HOH1105 |
| E | HOH1107 |
| E | HOH1108 |
| E | HOH1112 |
| E | HOH1113 |
| E | HOH1114 |
| E | HOH1117 |
| site_id | AC6 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 112 F 1201 |
| Chain | Residue |
| B | LEU248 |
| B | GLY250 |
| B | GLY251 |
| B | GLN252 |
| B | TYR253 |
| B | GLY254 |
| B | VAL256 |
| B | ALA269 |
| B | LYS271 |
| B | THR315 |
| B | GLU316 |
| B | PHE317 |
| B | MET318 |
| B | ASN322 |
| B | ASP363 |
| B | ARG367 |
| B | ASN368 |
| B | LEU370 |
| B | ASP381 |
| B | MG1601 |
| B | HOH1610 |
| B | HOH1637 |
| F | PHE107 |
| F | HOH129 |
| F | HOH200 |
| F | HOH223 |
| F | HOH262 |
| F | HOH268 |
| F | HOH269 |
| F | HOH306 |
| F | HOH536 |
| F | HOH661 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE 112 G 1301 |
| Chain | Residue |
| C | ASN368 |
| C | LEU370 |
| C | ASP381 |
| C | MG1701 |
| C | HOH1711 |
| C | HOH1721 |
| C | HOH1795 |
| C | HOH1801 |
| G | HOH7 |
| G | PHE107 |
| G | HOH143 |
| G | HOH323 |
| G | HOH326 |
| G | HOH489 |
| G | HOH586 |
| G | HOH991 |
| C | LEU248 |
| C | GLY250 |
| C | GLY251 |
| C | GLN252 |
| C | TYR253 |
| C | GLY254 |
| C | VAL256 |
| C | ALA269 |
| C | LYS271 |
| C | THR315 |
| C | GLU316 |
| C | PHE317 |
| C | MET318 |
| C | ASN322 |
| C | ARG367 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE 112 H 1401 |
| Chain | Residue |
| D | LEU248 |
| D | GLY250 |
| D | GLY251 |
| D | GLN252 |
| D | TYR253 |
| D | GLY254 |
| D | VAL256 |
| D | ALA269 |
| D | LYS271 |
| D | THR315 |
| D | GLU316 |
| D | PHE317 |
| D | MET318 |
| D | ASN322 |
| D | ASP363 |
| D | ARG367 |
| D | ASN368 |
| D | LEU370 |
| D | ASP381 |
| D | MG1801 |
| D | HOH1810 |
| D | HOH1812 |
| D | HOH1928 |
| H | PHE107 |
| H | HOH1402 |
| H | HOH1403 |
| H | HOH1404 |
| H | HOH1405 |
| H | HOH1406 |
| H | HOH1408 |
| H | HOH1410 |
| H | HOH1412 |
| H | HOH1413 |
| H | HOH1415 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK |
| Chain | Residue | Details |
| A | LEU248-LYS271 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
| Chain | Residue | Details |
| A | PHE359-VAL371 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP363 | |
| B | ASP363 | |
| C | ASP363 | |
| D | ASP363 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU248 | |
| D | LEU248 | |
| D | LYS271 | |
| D | GLU316 | |
| A | LYS271 | |
| A | GLU316 | |
| B | LEU248 | |
| B | LYS271 | |
| B | GLU316 | |
| C | LEU248 | |
| C | LYS271 | |
| C | GLU316 | |
| Chain | Residue | Details |
| A | SER229 | |
| B | SER229 | |
| C | SER229 | |
| D | SER229 | |
| Chain | Residue | Details |
| A | TYR253 | |
| D | TYR253 | |
| D | TYR257 | |
| D | TYR413 | |
| A | TYR257 | |
| A | TYR413 | |
| B | TYR253 | |
| B | TYR257 | |
| B | TYR413 | |
| C | TYR253 | |
| C | TYR257 | |
| C | TYR413 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 |
| Chain | Residue | Details |
| A | TYR393 | |
| B | TYR393 | |
| C | TYR393 | |
| D | TYR393 | |
| Chain | Residue | Details |
| A | SER446 | |
| B | SER446 | |
| C | SER446 | |
| D | SER446 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP363 | |
| A | ARG367 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP363 | |
| B | ARG367 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP363 | |
| C | ARG367 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP363 | |
| D | ARG367 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP363 | |
| A | ALA365 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP363 | |
| B | ALA365 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP363 | |
| C | ALA365 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP363 | |
| D | ALA365 | |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN368 | |
| A | ASP363 | |
| A | ALA365 | |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN368 | |
| B | ASP363 | |
| B | ALA365 | |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASN368 | |
| C | ASP363 | |
| C | ALA365 | |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASN368 | |
| D | ASP363 | |
| D | ALA365 | |
