Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0046777 | biological_process | protein autophosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0046777 | biological_process | protein autophosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE D15 A 600 |
Chain | Residue |
A | ILE165 |
A | ASN292 |
A | LEU294 |
A | ASP307 |
A | HOH2191 |
A | GLY168 |
A | GLY171 |
A | ALA186 |
A | LYS188 |
A | GLU239 |
A | MET240 |
A | LEU241 |
A | SER242 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE D15 B 600 |
Chain | Residue |
B | ILE165 |
B | LYS167 |
B | GLY168 |
B | GLY171 |
B | ALA186 |
B | LYS188 |
B | GLU239 |
B | MET240 |
B | LEU241 |
B | SER242 |
B | ASN292 |
B | LEU294 |
B | ASP307 |
B | CL700 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 700 |
Chain | Residue |
B | LYS188 |
B | D15600 |
B | HOH2043 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydrveqew..........VAIK |
Chain | Residue | Details |
A | ILE165-LYS188 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL |
Chain | Residue | Details |
A | ILE283-LEU295 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP287 | |
B | ASP287 | |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ILE165 | |
A | LYS188 | |
A | PHE238 | |
B | ILE165 | |
B | LYS188 | |
B | PHE238 | |
Chain | Residue | Details |
A | TYR140 | |
B | TYR319 | |
B | PTR321 | |
B | TYR449 | |
A | TYR159 | |
A | TYR177 | |
A | TYR319 | |
A | PTR321 | |
A | TYR449 | |
B | TYR140 | |
B | TYR159 | |
B | TYR177 | |
Chain | Residue | Details |
A | TYR145 | |
B | TYR145 | |
Chain | Residue | Details |
A | TYR219 | |
B | TYR219 | |
Chain | Residue | Details |
A | SER310 | |
B | SER310 | |
Chain | Residue | Details |
A | THR402 | |
B | THR402 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLU291 | |
A | ASP287 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | GLU291 | |
B | ASP287 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP287 | |
A | LYS289 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP287 | |
B | LYS289 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP287 | |
A | SER324 | |
A | LYS289 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP287 | |
B | SER324 | |
B | LYS289 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN292 | |
A | ASP287 | |
A | LYS289 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN292 | |
B | ASP287 | |
B | LYS289 | |