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 | 15 |
Details | binding site for residue F6J A 501 |
Chain | Residue |
A | ILE171 |
A | PRO274 |
A | LEU319 |
A | ASP330 |
A | HOH612 |
A | HOH633 |
A | HOH670 |
A | GLY174 |
A | VAL179 |
A | ALA192 |
A | LYS194 |
A | PHE267 |
A | GLU268 |
A | LEU269 |
A | VAL270 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue FMT A 502 |
Chain | Residue |
A | LYS200 |
A | GLN204 |
A | PRO279 |
A | GLN387 |
A | CYS388 |
A | HOH669 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue FMT A 503 |
Chain | Residue |
A | GLY177 |
A | LEU196 |
A | SER197 |
A | LYS200 |
A | HOH630 |
A | HOH651 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue FMT A 504 |
Chain | Residue |
A | GLU277 |
A | VAL278 |
A | LYS314 |
A | PRO315 |
A | SER316 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LEU269 |
A | ASN271 |
A | GLY321 |
A | GLU322 |
A | HOH602 |
A | HOH618 |
A | HOH632 |
B | TYR183 |
B | ASN188 |
site_id | AC6 |
Number of Residues | 15 |
Details | binding site for residue F6J B 501 |
Chain | Residue |
B | ILE171 |
B | GLY174 |
B | VAL179 |
B | ALA192 |
B | LYS194 |
B | PHE267 |
B | GLU268 |
B | LEU269 |
B | VAL270 |
B | ASN317 |
B | LEU319 |
B | ASP330 |
B | HOH614 |
B | HOH628 |
B | HOH643 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue FMT B 502 |
Chain | Residue |
B | LYS200 |
B | GLN204 |
B | PRO279 |
B | GLN387 |
B | CYS388 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue FMT B 503 |
Chain | Residue |
B | GLY177 |
B | LEU196 |
B | SER197 |
B | LYS200 |
B | HOH655 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue FMT B 504 |
Chain | Residue |
B | GLU277 |
B | VAL278 |
B | LYS314 |
B | PRO315 |
B | SER316 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | THR350 |
B | HOH657 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
A | TYR183 |
A | ASN188 |
A | HOH654 |
B | LEU269 |
B | ASN271 |
B | GLU322 |
B | HOH653 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSYGVVKlAynendnty..........YAMK |
Chain | Residue | Details |
A | ILE171-LYS194 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDIKpsNLLV |
Chain | Residue | Details |
A | ILE308-VAL320 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
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_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |