8F5J
human branched chain ketoacid dehydrogenase kinase in complex with inhibitors
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 | 0004722 | molecular_function | protein serine/threonine phosphatase 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 | 0008610 | biological_process | lipid biosynthetic process |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0009083 | biological_process | branched-chain amino acid catabolic process |
A | 0010906 | biological_process | regulation of glucose metabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
A | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
A | 0045763 | biological_process | negative regulation of cellular amino acid metabolic process |
A | 0047323 | molecular_function | [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity |
A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37558654, ECO:0007744|PDB:8F5J, ECO:0007744|PDB:8F5S |
Chain | Residue | Details |
A | ASN249 | |
A | VAL298 | |
A | ASP300 | |
A | PHE303 | |
A | GLY337 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37558654, ECO:0007744|PDB:8F5J |
Chain | Residue | Details |
A | ASP285 | |
A | THR304 | |
A | THR305 | |
A | HIS334 | |
A | LEU340 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q00972 |
Chain | Residue | Details |
A | SER1 | |
A | SER330 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250 |
Chain | Residue | Details |
A | SER22 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS162 | |
A | LYS203 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O55028 |
Chain | Residue | Details |
A | SER326 |