4MP7
Crystal structure of pyruvate dehydrogenase kinase isoform 2 in complex with inhibitor PA7
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| 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 pyruvate decarboxylation to acetyl-CoA |
| A | 0010565 | biological_process | regulation of ketone metabolic process |
| A | 0010906 | biological_process | regulation of glucose metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0031670 | biological_process | cellular response to nutrient |
| A | 0033554 | biological_process | cellular response to stress |
| 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 | 0072332 | biological_process | intrinsic apoptotic signaling pathway by p53 class mediator |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PFT A 501 |
| Chain | Residue |
| A | LEU252 |
| A | THR354 |
| A | HOH602 |
| A | HOH617 |
| A | ASN255 |
| A | ARG258 |
| A | ALA259 |
| A | GLU262 |
| A | ASP290 |
| A | GLY294 |
| A | VAL295 |
| A | LEU346 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TLA A 502 |
| Chain | Residue |
| A | GLU262 |
| A | SER263 |
| A | HIS264 |
| A | GLU265 |
| A | SER266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16401071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q15118","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BFP9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
