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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 601 |
Chain | Residue |
A | PRO429 |
A | SER430 |
A | ARG481 |
A | HOH702 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 396 A 901 |
Chain | Residue |
A | ASN376 |
A | GLU377 |
A | TYR378 |
A | CYS379 |
A | ASN380 |
A | GLY382 |
A | PHE433 |
A | HOH605 |
A | HOH685 |
A | HOH691 |
A | ILE305 |
A | ALA326 |
A | LYS328 |
A | GLU346 |
A | VAL360 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGEFGSVFkCvkrldgci..........YAIK |
Chain | Residue | Details |
A | ILE305-LYS328 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHmDIKpsNIFI |
Chain | Residue | Details |
A | LEU422-ILE434 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP426 | |
Chain | Residue | Details |
A | ILE305 | |
A | LYS328 | |
Chain | Residue | Details |
A | ASN342 | |
A | ASN431 | |
A | ASP463 | |
A | GLY465 | |
Chain | Residue | Details |
A | SER307 | |
Chain | Residue | Details |
A | SER312 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP426 | |
A | SER430 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS428 | |
A | ASP426 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN431 | |
A | LYS428 | |
A | ASP426 | |