1GKZ
Branched-chain alpha-ketoacid dehydrogenase kinase (BCK) complxed with ADP
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 | 0005524 | molecular_function | ATP binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006550 | biological_process | isoleucine catabolic process |
A | 0006552 | biological_process | L-leucine catabolic process |
A | 0006574 | biological_process | 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 | 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 | 0047323 | molecular_function | [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity |
A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ASN249 |
A | HIS334 |
A | ADP601 |
A | HOH2072 |
A | HOH2100 |
A | HOH2124 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 402 |
Chain | Residue |
A | GLY337 |
A | PRO341 |
A | ADP601 |
A | VAL298 |
A | ASP300 |
A | PHE303 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 701 |
Chain | Residue |
A | ILE235 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 702 |
Chain | Residue |
A | HOH2009 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 502 |
Chain | Residue |
A | HIS132 |
site_id | AC6 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ADP A 601 |
Chain | Residue |
A | ASN249 |
A | ARG252 |
A | ALA253 |
A | ASP285 |
A | GLY289 |
A | ILE290 |
A | VAL298 |
A | THR304 |
A | THR305 |
A | HIS334 |
A | PHE336 |
A | GLY337 |
A | GLY339 |
A | LEU340 |
A | PRO341 |
A | THR364 |
A | MG401 |
A | K402 |
A | HOH2091 |
A | HOH2100 |
A | HOH2122 |
A | HOH2123 |
A | HOH2124 |
A | HOH2125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11562470, ECO:0007744|PDB:1GKZ |
Chain | Residue | Details |
A | ASN249 | |
A | LEU340 | |
A | ASP285 | |
A | VAL298 | |
A | ASP300 | |
A | PHE303 | |
A | THR304 | |
A | THR305 | |
A | HIS334 | |
A | GLY337 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7649998, ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER1 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O14874 |
Chain | Residue | Details |
A | LYS162 | |
A | LYS203 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER326 | |
A | SER330 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1jm6 |
Chain | Residue | Details |
A | GLU245 | |
A | TYR241 |