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 | 3 |
| Details | binding site for residue IOD A 502 |
| Chain | Residue |
| A | ASN203 |
| A | LYS206 |
| B | ASN227 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 503 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue IOD A 504 |
| Chain | Residue |
| A | HIS143 |
| A | LEU144 |
| A | ILE187 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 505 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 506 |
| Chain | Residue |
| A | HOH620 |
| A | LEU221 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 507 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | PHE244 |
| A | LYS248 |
| A | HOH606 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | LYS186 |
| A | ASP320 |
| A | E6Q511 |
| A | HOH611 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | PHE371 |
| A | HOH614 |
| A | HOH617 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue E6Q A 511 |
| Chain | Residue |
| A | LEU162 |
| A | GLY163 |
| A | GLU164 |
| A | VAL170 |
| A | ALA184 |
| A | PHE236 |
| A | GLU237 |
| A | LEU239 |
| A | EDO509 |
| A | HOH706 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue IOD B 501 |
| Chain | Residue |
| A | ASN227 |
| B | ASN203 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 502 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 503 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 504 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue IOD B 505 |
| Chain | Residue |
| B | HIS143 |
| B | LEU144 |
| B | ILE187 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue IOD B 507 |
| Chain | Residue |
| B | LYS209 |
| B | SER223 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 508 |
| Chain | Residue |
| A | LYS206 |
| A | TRP225 |
| B | LYS206 |
| B | TRP225 |
| B | HOH601 |
| B | HOH608 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 509 |
| Chain | Residue |
| B | LYS248 |
| B | PHE252 |
| B | HOH611 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 510 |
| Chain | Residue |
| A | ASP327 |
| B | SER133 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 511 |
| Chain | Residue |
| B | HIS259 |
| B | VAL311 |
| B | LYS312 |
| B | HOH624 |
| B | HOH709 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 512 |
| Chain | Residue |
| B | LYS186 |
| B | ASP320 |
| B | E6Q517 |
| B | HOH675 |
| B | HOH789 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 513 |
| Chain | Residue |
| A | ARG199 |
| A | TRP225 |
| B | ARG199 |
| site_id | AE5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 514 |
| Chain | Residue |
| B | ASP327 |
| B | HOH674 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 515 |
| Chain | Residue |
| B | PRO254 |
| B | GLU308 |
| B | LEU436 |
| B | HOH688 |
| B | HOH736 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 516 |
| Chain | Residue |
| B | ARG380 |
| B | VAL413 |
| B | TRP414 |
| B | ASP415 |
| site_id | AE8 |
| Number of Residues | 10 |
| Details | binding site for residue E6Q B 517 |
| Chain | Residue |
| B | GLY163 |
| B | GLU164 |
| B | VAL170 |
| B | ALA184 |
| B | PHE236 |
| B | GLU237 |
| B | LEU238 |
| B | LEU239 |
| B | EDO512 |
| B | HOH653 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTFGKVVeCldhargksq.........VALK |
| Chain | Residue | Details |
| A | LEU162-LYS186 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF |
| Chain | Residue | Details |
| A | LEU279-PHE291 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 632 |
| 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"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
