2Q8I
Pyruvate dehydrogenase kinase isoform 3 in complex with antitumor drug radicicol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004740 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0010510 | biological_process | regulation of pyruvate decarboxylation to acetyl-CoA |
| A | 0010906 | biological_process | regulation of glucose metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0033554 | biological_process | cellular response to stress |
| A | 0035357 | biological_process | peroxisome proliferator activated receptor signaling pathway |
| A | 0071333 | biological_process | cellular response to glucose stimulus |
| A | 0071398 | biological_process | cellular response to fatty acid |
| A | 0097411 | biological_process | hypoxia-inducible factor-1alpha signaling pathway |
| A | 2000377 | biological_process | regulation of reactive oxygen species metabolic process |
| B | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| B | 0045254 | cellular_component | pyruvate dehydrogenase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 407 |
| Chain | Residue |
| A | SER20 |
| A | ARG21 |
| A | PHE22 |
| A | ASN59 |
| A | PHE372 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE RED B 300 |
| Chain | Residue |
| A | PHE48 |
| A | ARG397 |
| B | LYS173 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RDC A 408 |
| Chain | Residue |
| A | ASN251 |
| A | SER252 |
| A | ALA255 |
| A | ASP287 |
| A | VAL292 |
| A | LEU300 |
| A | LEU328 |
| A | THR352 |
| A | HOH431 |
| A | HOH453 |
| A | HOH475 |
| A | LEU248 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 409 |
| Chain | Residue |
| A | PHE301 |
| A | LYS343 |
| A | LYS343 |
| A | LEU344 |
| A | TYR345 |
| A | TYR345 |
| A | HOH419 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV |
| Chain | Residue | Details |
| B | PRO138-VAL149 |
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL |
| Chain | Residue | Details |
| B | GLY157-LEU186 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q922H2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 76 |
| Details | Domain: {"description":"Lipoyl-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17532006","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17683942","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25525879","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PNR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Q8I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jm6 |
| Chain | Residue | Details |
| A | HIS243 | |
| A | GLU247 |
