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 |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
C | 0046777 | biological_process | protein autophosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
D | 0046777 | biological_process | protein autophosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue QKG A 501 |
Chain | Residue |
A | ILE165 |
A | LEU294 |
A | ASP307 |
A | PHE170 |
A | ALA186 |
A | LYS188 |
A | PHE238 |
A | GLU239 |
A | MET240 |
A | LEU241 |
A | ASN244 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue PG4 A 502 |
Chain | Residue |
A | TYR319 |
A | PTR321 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PG4 A 503 |
Chain | Residue |
A | GLY419 |
A | LYS422 |
B | ARG458 |
B | TYR472 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue PG4 A 504 |
Chain | Residue |
A | GLN201 |
C | GLN201 |
site_id | AC5 |
Number of Residues | 12 |
Details | binding site for residue QKG B 501 |
Chain | Residue |
B | ILE165 |
B | PHE170 |
B | LYS188 |
B | PHE238 |
B | GLU239 |
B | MET240 |
B | LEU241 |
B | SER242 |
B | ASN244 |
B | LEU294 |
B | ASP307 |
D | GLN182 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PG4 B 502 |
Chain | Residue |
B | ASP162 |
B | LYS175 |
B | TRP184 |
B | MET240 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue PG4 B 503 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue PG4 B 504 |
Chain | Residue |
A | ARG458 |
A | GLN475 |
B | LYS422 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue QKG C 501 |
Chain | Residue |
C | ILE165 |
C | PHE170 |
C | ALA186 |
C | LYS188 |
C | PHE238 |
C | GLU239 |
C | LEU241 |
C | ASN244 |
C | LEU294 |
C | ASP307 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue PG4 C 502 |
Chain | Residue |
C | ASP162 |
C | LYS175 |
C | TRP184 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue PG4 C 503 |
Chain | Residue |
C | TYR319 |
C | PTR321 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue QKG D 501 |
Chain | Residue |
D | PHE170 |
D | ALA186 |
D | LYS188 |
D | PHE238 |
D | GLU239 |
D | LEU241 |
D | ASN244 |
D | GLU291 |
D | LEU294 |
D | ASP307 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue PG4 D 502 |
Chain | Residue |
D | ASP162 |
D | LYS175 |
D | TRP184 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue PG4 D 503 |
Chain | Residue |
D | PHE196 |
D | TYR319 |
D | PTR321 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue PG4 D 504 |
Chain | Residue |
B | GLN201 |
B | HIS227 |
B | LEU234 |
D | GLN201 |
D | HIS227 |
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 | |
C | ASP287 | |
D | ASP287 | |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ILE165 | |
D | ILE165 | |
D | LYS188 | |
D | PHE238 | |
A | LYS188 | |
A | PHE238 | |
B | ILE165 | |
B | LYS188 | |
B | PHE238 | |
C | ILE165 | |
C | LYS188 | |
C | PHE238 | |
Chain | Residue | Details |
A | TYR140 | |
B | TYR319 | |
B | PTR321 | |
B | TYR449 | |
C | TYR140 | |
C | TYR159 | |
C | TYR177 | |
C | TYR319 | |
C | PTR321 | |
C | TYR449 | |
D | TYR140 | |
A | TYR159 | |
D | TYR159 | |
D | TYR177 | |
D | TYR319 | |
D | PTR321 | |
D | TYR449 | |
A | TYR177 | |
A | TYR319 | |
A | PTR321 | |
A | TYR449 | |
B | TYR140 | |
B | TYR159 | |
B | TYR177 | |
Chain | Residue | Details |
A | TYR145 | |
B | TYR145 | |
C | TYR145 | |
D | TYR145 | |
Chain | Residue | Details |
A | TYR219 | |
B | TYR219 | |
C | TYR219 | |
D | TYR219 | |
Chain | Residue | Details |
A | SER310 | |
B | SER310 | |
C | SER310 | |
D | SER310 | |
Chain | Residue | Details |
A | THR402 | |
B | THR402 | |
C | THR402 | |
D | THR402 | |