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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue DMS A 801 |
| Chain | Residue |
| A | HIS568 |
| A | PHE635 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue DMS A 802 |
| Chain | Residue |
| B | 6NB801 |
| A | GLY464 |
| A | SER465 |
| A | GLY466 |
| A | ASN580 |
| A | HOH927 |
| A | HOH929 |
| A | HOH969 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue DMS A 803 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue BEN A 804 |
| Chain | Residue |
| A | TRP450 |
| A | ARG509 |
| A | PHE516 |
| A | MET517 |
| D | ASP449 |
| D | TRP450 |
| D | GLU451 |
| D | MET517 |
| D | CL802 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EOH A 805 |
| Chain | Residue |
| A | ASP587 |
| D | GLY455 |
| site_id | AC6 |
| Number of Residues | 39 |
| Details | binding site for residue 6NB B 801 |
| Chain | Residue |
| A | GLN461 |
| A | ILE463 |
| A | VAL471 |
| A | ALA481 |
| A | LYS483 |
| A | LEU514 |
| A | THR529 |
| A | GLN530 |
| A | TRP531 |
| A | CYS532 |
| A | SER535 |
| A | HIS539 |
| A | PHE583 |
| A | GLY593 |
| A | ASP594 |
| A | PHE595 |
| A | GLY596 |
| A | DMS802 |
| A | HOH927 |
| B | GLN461 |
| B | ILE463 |
| B | VAL471 |
| B | ALA481 |
| B | LYS483 |
| B | LEU514 |
| B | THR529 |
| B | GLN530 |
| B | TRP531 |
| B | CYS532 |
| B | SER535 |
| B | HIS539 |
| B | PHE583 |
| B | GLY593 |
| B | ASP594 |
| B | PHE595 |
| B | GLY596 |
| B | DMS802 |
| B | HOH911 |
| B | HOH926 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 802 |
| Chain | Residue |
| B | GLY464 |
| B | SER465 |
| B | VAL471 |
| B | 6NB801 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 803 |
| Chain | Residue |
| B | PHE447 |
| B | LYS499 |
| B | VAL502 |
| B | GLY503 |
| B | ARG506 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EOH B 805 |
| Chain | Residue |
| B | LEU485 |
| B | VAL487 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 806 |
| Chain | Residue |
| B | LYS507 |
| B | TYR566 |
| B | LYS570 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue BEN B 807 |
| Chain | Residue |
| B | ASP449 |
| B | TRP450 |
| B | MET517 |
| B | CL808 |
| C | TRP450 |
| C | ARG509 |
| C | MET517 |
| C | HOH938 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 808 |
| Chain | Residue |
| B | TRP450 |
| B | PHE516 |
| B | BEN807 |
| C | HOH938 |
| site_id | AD4 |
| Number of Residues | 36 |
| Details | binding site for residue 6NB C 801 |
| Chain | Residue |
| C | PHE583 |
| C | GLY593 |
| C | ASP594 |
| C | PHE595 |
| C | GLY596 |
| C | DMS802 |
| C | HOH917 |
| D | GLN461 |
| D | ILE463 |
| D | VAL471 |
| D | ALA481 |
| D | LYS483 |
| D | LEU514 |
| D | THR529 |
| D | GLN530 |
| D | TRP531 |
| D | CYS532 |
| D | SER535 |
| D | PHE583 |
| D | GLY593 |
| D | ASP594 |
| D | PHE595 |
| D | GLY596 |
| D | HOH929 |
| C | GLN461 |
| C | ILE463 |
| C | VAL471 |
| C | ALA481 |
| C | LYS483 |
| C | LEU514 |
| C | THR529 |
| C | GLN530 |
| C | TRP531 |
| C | CYS532 |
| C | SER535 |
| C | HIS539 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 802 |
| Chain | Residue |
| C | ILE463 |
| C | HIS539 |
| C | 6NB801 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS D 801 |
| Chain | Residue |
| D | SER465 |
| D | ASN580 |
| D | HOH929 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 802 |
| Chain | Residue |
| A | BEN804 |
| A | HOH960 |
| D | TRP450 |
| D | PHE516 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 21 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK |
| Chain | Residue | Details |
| A | ILE463-LYS483 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL |
| Chain | Residue | Details |
| A | ILE572-LEU584 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Omega-N-methylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23907581","evidenceCode":"ECO:0000269"}]} |
