3VAD
Crystal structure of I170F mutant branched-chain alpha-ketoacid dehydrogenase kinase in complex with 3,6-dichlorobenzo[b]thiophene-2-carboxylic acid
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 | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0004740 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006550 | biological_process | L-isoleucine catabolic process |
| A | 0006552 | biological_process | L-leucine catabolic process |
| A | 0006574 | biological_process | L-valine catabolic process |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| 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 | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
| A | 0047323 | molecular_function | [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 0140096 | molecular_function | catalytic activity, acting on a protein |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP A 401 |
| Chain | Residue |
| A | ASN249 |
| A | GLY335 |
| A | PHE336 |
| A | GLY337 |
| A | GLY339 |
| A | LEU340 |
| A | PRO341 |
| A | THR364 |
| A | MG402 |
| A | K403 |
| A | HOH501 |
| A | ARG252 |
| A | HOH502 |
| A | ALA253 |
| A | ASP285 |
| A | GLY289 |
| A | ILE290 |
| A | VAL298 |
| A | THR304 |
| A | THR305 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ASN249 |
| A | ADP401 |
| A | HOH501 |
| A | HOH502 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 403 |
| Chain | Residue |
| A | VAL298 |
| A | ASP300 |
| A | PHE303 |
| A | GLY337 |
| A | PRO341 |
| A | ADP401 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 0F1 A 404 |
| Chain | Residue |
| A | LEU68 |
| A | ILE72 |
| A | TYR99 |
| A | VAL125 |
| A | LEU128 |
| A | LEU129 |
| A | HIS132 |
| A | ARG167 |
| A | PHE170 |
| A | ARG171 |
| A | 0F1405 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 0F1 A 405 |
| Chain | Residue |
| A | ARG71 |
| A | ILE72 |
| A | ARG75 |
| A | TYR99 |
| A | HIS132 |
| A | SER166 |
| A | ARG167 |
| A | PHE170 |
| A | 0F1404 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11562470","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GKZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O14874","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
