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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 4ST B 501 |
Chain | Residue |
B | LEU248 |
B | LEU370 |
B | ASP381 |
B | ALA269 |
B | LYS271 |
B | THR315 |
B | GLU316 |
B | PHE317 |
B | MET318 |
B | GLY321 |
B | ARG367 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 4ST A 501 |
Chain | Residue |
A | TRP235 |
A | TRP261 |
A | TYR264 |
A | LYS294 |
A | LEU302 |
C | TYR342 |
C | PHE497 |
C | GLN498 |
C | SER500 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 4ST C 501 |
Chain | Residue |
A | TYR342 |
A | PHE497 |
A | GLN498 |
A | SER500 |
C | TRP235 |
C | TYR264 |
C | GLN300 |
C | LEU302 |
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 | |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU248 | |
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 | |
Chain | Residue | Details |
A | TYR253 | |
A | TYR257 | |
A | TYR413 | |
B | TYR253 | |
B | TYR257 | |
B | TYR413 | |
C | TYR253 | |
C | TYR257 | |
C | TYR413 | |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 |
Chain | Residue | Details |
A | TYR393 | |
B | TYR393 | |
C | TYR393 | |
Chain | Residue | Details |
A | SER446 | |
B | SER446 | |
C | 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 |
A | ASP363 | |
A | ALA365 | |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP363 | |
B | ALA365 | |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASP363 | |
C | ALA365 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN368 | |
A | ASP363 | |
A | ALA365 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN368 | |
B | ASP363 | |
B | ALA365 | |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASN368 | |
C | ASP363 | |
C | ALA365 | |