7EBH
Crystal structure of human pyruvate dehydrogenase kinase 2 in complex with compound 13
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein 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 | 0005654 | cellular_component | nucleoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006111 | biological_process | regulation of gluconeogenesis |
| A | 0006885 | biological_process | regulation of pH |
| A | 0008286 | biological_process | insulin receptor signaling pathway |
| A | 0010510 | biological_process | regulation of acetyl-CoA biosynthetic process from pyruvate |
| A | 0010565 | biological_process | regulation of cellular ketone metabolic process |
| A | 0010906 | biological_process | regulation of glucose metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0031670 | biological_process | cellular response to nutrient |
| A | 0034614 | biological_process | cellular response to reactive oxygen species |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045254 | cellular_component | pyruvate dehydrogenase complex |
| A | 0050848 | biological_process | regulation of calcium-mediated signaling |
| A | 0072332 | biological_process | intrinsic apoptotic signaling pathway by p53 class mediator |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | TYR88 |
| A | HIS123 |
| A | VAL126 |
| A | ARG162 |
| A | ACT503 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 502 |
| Chain | Residue |
| A | ARG162 |
| A | ILE163 |
| A | TYR336 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | ILE165 |
| A | ARG166 |
| A | CL501 |
| A | HIS123 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 504 |
| Chain | Residue |
| A | PHE36 |
| A | PHE39 |
| A | SER49 |
| A | PHE52 |
| A | HOH604 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue DMS A 505 |
| Chain | Residue |
| A | VAL81 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue J0F A 506 |
| Chain | Residue |
| A | ASN255 |
| A | ALA259 |
| A | MET288 |
| A | ASP290 |
| A | GLY294 |
| A | VAL295 |
| A | LEU330 |
| A | THR354 |
| A | ALA356 |
| A | HOH631 |
| A | HOH641 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16401071 |
| Chain | Residue | Details |
| A | GLU251 | |
| A | ASP290 | |
| A | GLY325 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER309 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q15118 |
| Chain | Residue | Details |
| A | TYR215 | |
| A | TYR216 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8BFP9 |
| Chain | Residue | Details |
| A | LYS376 |
