1Y8O
Crystal structure of the PDK3-L2 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0005730 | cellular_component | nucleolus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0010510 | biological_process | regulation of acetyl-CoA biosynthetic process from pyruvate |
| A | 0010906 | biological_process | regulation of glucose metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| 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 | acetyl-CoA biosynthetic process from pyruvate |
| B | 0045254 | cellular_component | pyruvate dehydrogenase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | GLU247 |
| A | LYS250 |
| A | ASN251 |
| A | ADP504 |
| A | HOH544 |
| A | HOH560 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 502 |
| Chain | Residue |
| A | GLY325 |
| A | ADP504 |
| A | LEU300 |
| A | ASN302 |
| A | SER306 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| Chain | Residue |
| A | SER20 |
| A | ARG21 |
| A | PHE22 |
| A | ASN59 |
| A | PHE372 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE RED B 373 |
| Chain | Residue |
| A | SER45 |
| A | PHE48 |
| B | LYS173 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 504 |
| Chain | Residue |
| A | ASN251 |
| A | ARG254 |
| A | ALA255 |
| A | ASP287 |
| A | VAL292 |
| A | LEU300 |
| A | PHE324 |
| A | GLY325 |
| A | LEU328 |
| A | THR352 |
| A | MG501 |
| A | K502 |
| A | HOH514 |
| A | HOH531 |
| A | HOH544 |
| A | HOH560 |
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 | 1 |
| Details | MOD_RES: N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I |
| Chain | Residue | Details |
| B | ILE206 | |
| A | ASP287 | |
| A | SER306 | |
| A | GLY323 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q922H2 |
| Chain | Residue | Details |
| A | LYS278 |
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 |
