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 | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1710 |
| Chain | Residue |
| B | GLY467 |
| B | HIS469 |
| B | ILE472 |
| B | THR474 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1711 |
| Chain | Residue |
| B | THR612 |
| B | PRO613 |
| B | PHE614 |
| B | ALA615 |
| B | THR701 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1709 |
| Chain | Residue |
| A | GLY467 |
| A | HIS469 |
| A | ILE472 |
| A | THR474 |
| A | HOH2011 |
| A | HOH2012 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1712 |
| Chain | Residue |
| B | LEU502 |
| B | MET607 |
| B | SER687 |
| B | HIS688 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 1713 |
| Chain | Residue |
| B | THR627 |
| B | ARG628 |
| B | SER631 |
| B | GLN683 |
| B | HOH2062 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG B 1714 |
| Chain | Residue |
| B | GLU496 |
| B | LEU497 |
| B | LEU498 |
| B | LYS537 |
| B | PRO538 |
| B | SER539 |
| B | MET698 |
| B | HOH2122 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGVGSYSECKrCvhkatnme..........YAVK |
| Chain | Residue | Details |
| A | ILE424-LYS447 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpsNILY |
| Chain | Residue | Details |
| A | VAL531-TYR543 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"9430688","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP535 | |
| A | SER539 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP535 | |
| B | SER539 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP535 | |
| A | LYS537 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP535 | |
| B | LYS537 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR577 | |
| A | ASP535 | |
| A | LYS537 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN540 | |
| A | ASP535 | |
| A | LYS537 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN540 | |
| B | ASP535 | |
| B | LYS537 | |
