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 | 8 |
Details | BINDING SITE FOR RESIDUE AWR A 900 |
Chain | Residue |
A | PHE170 |
A | VAL173 |
A | LYS188 |
A | GLU203 |
A | PHE238 |
A | GLU239 |
A | LEU241 |
A | ASP307 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AWR B 900 |
Chain | Residue |
B | PHE170 |
B | VAL173 |
B | ALA186 |
B | LYS188 |
B | GLU203 |
B | PHE238 |
B | GLU239 |
B | LEU241 |
B | SER242 |
B | LEU294 |
B | ASP307 |
B | GLY166 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AWR C 900 |
Chain | Residue |
C | LYS167 |
C | PHE170 |
C | VAL173 |
C | ALA186 |
C | LYS188 |
C | PHE238 |
C | GLU239 |
C | LEU241 |
C | ASP307 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AWR D 900 |
Chain | Residue |
D | ILE165 |
D | PHE170 |
D | VAL173 |
D | ALA186 |
D | LYS188 |
D | GLU203 |
D | PHE238 |
D | GLU239 |
D | LEU241 |
D | SER242 |
D | LEU294 |
D | ASP307 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 1483 |
Chain | Residue |
B | GLY168 |
B | SER169 |
C | TYR145 |
C | LYS193 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 1484 |
Chain | Residue |
B | LYS193 |
B | LYS194 |
C | SER310 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 1483 |
Chain | Residue |
B | TYR145 |
B | LYS193 |
C | GLY168 |
C | SER169 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 1483 |
Chain | Residue |
A | GLY168 |
A | SER169 |
D | TYR145 |
D | LYS193 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 D 1482 |
Chain | Residue |
A | SER310 |
D | LYS193 |
D | LYS194 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 D 1483 |
Chain | Residue |
A | TYR145 |
D | GLY168 |
D | SER169 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 1484 |
Chain | Residue |
A | LYS264 |
A | ARG300 |
A | SER301 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 1485 |
Chain | Residue |
B | LYS264 |
B | ARG300 |
B | SER301 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 C 1484 |
Chain | Residue |
C | LYS264 |
C | ARG300 |
C | SER301 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 D 1484 |
Chain | Residue |
D | LYS264 |
D | ARG300 |
D | SER301 |
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 | |