Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ADP A 301 |
Chain | Residue |
A | GLY16 |
A | LEU85 |
A | LEU135 |
A | ILE148 |
A | ASP149 |
A | HOH424 |
A | HOH436 |
A | HOH440 |
A | HOH453 |
A | GLY18 |
A | ILE23 |
A | ALA36 |
A | LYS38 |
A | GLU52 |
A | TYR56 |
A | MET82 |
A | GLU83 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | ARG10 |
A | LEU11 |
A | GLY12 |
A | LEU25 |
A | GLY26 |
A | THR27 |
A | GLU34 |
B | EDO307 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | ILE29 |
A | GLY32 |
B | PRO87 |
B | GLY137 |
B | TRP290 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | ILE15 |
A | LEU85 |
A | GLY86 |
A | PRO87 |
B | ARG10 |
B | GLU34 |
B | EDO306 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | PRO87 |
A | GLY142 |
A | TRP290 |
A | HOH428 |
B | ILE29 |
B | GLY32 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | ARG98 |
A | GLY209 |
A | HOH434 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | GLU117 |
A | HIS120 |
A | SER121 |
A | TYR156 |
A | ARG192 |
A | TYR266 |
A | HOH425 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO A 308 |
Chain | Residue |
A | TYR167 |
B | LYS242 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 309 |
Chain | Residue |
A | TYR201 |
A | TRP213 |
A | LYS232 |
A | THR235 |
A | ILE237 |
A | HOH402 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 310 |
Chain | Residue |
A | ASN253 |
A | ARG256 |
A | SER257 |
B | ASN253 |
B | SER257 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 311 |
Chain | Residue |
A | HIS278 |
A | PHE282 |
A | SER283 |
A | TYR284 |
B | TYR284 |
B | TYR286 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue NA A 312 |
Chain | Residue |
A | ASN143 |
A | TYR286 |
A | ASN291 |
A | HOH428 |
A | HOH480 |
A | HOH490 |
site_id | AD4 |
Number of Residues | 18 |
Details | binding site for residue ADP B 301 |
Chain | Residue |
B | SER17 |
B | GLY18 |
B | ILE23 |
B | ALA36 |
B | LYS38 |
B | GLU52 |
B | TYR56 |
B | MET82 |
B | GLU83 |
B | LEU85 |
B | ASP132 |
B | LEU135 |
B | ILE148 |
B | ASP149 |
B | HOH408 |
B | HOH423 |
B | HOH434 |
B | HOH476 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | ILE237 |
B | GLU238 |
B | ASN253 |
A | SER257 |
A | LEU258 |
B | PRO236 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | TYR268 |
B | GLN271 |
B | LEU272 |
B | HOH414 |
B | HOH424 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | ARG279 |
B | SER267 |
B | ARG270 |
B | GLN271 |
B | ARG274 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | TYR9 |
B | ARG69 |
B | TRP70 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue EDO B 306 |
Chain | Residue |
A | EDO304 |
A | HOH498 |
B | ARG10 |
B | GLY12 |
B | GLY26 |
B | THR27 |
B | GLU34 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue EDO B 307 |
Chain | Residue |
A | GLU34 |
A | EDO302 |
B | LEU85 |
B | GLY86 |
B | HOH407 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue EDO B 308 |
Chain | Residue |
B | VAL42 |
B | ASN78 |
B | SER101 |
B | LYS103 |
B | PHE282 |
B | HOH462 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGDIYlGtdiaagee..........VAIK |
Chain | Residue | Details |
A | ILE15-LYS38 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDVKpdNFLM |
Chain | Residue | Details |
A | PHE124-MET136 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 268 |
Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |