2J9F
Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase E1b
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003863 | molecular_function | branched-chain 2-oxo acid dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120552 | biological_process | branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA |
| A | 0160157 | cellular_component | branched-chain alpha-ketoacid dehydrogenase complex |
| C | 0003863 | molecular_function | branched-chain 2-oxo acid dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0009083 | biological_process | branched-chain amino acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0120552 | biological_process | branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA |
| C | 0160157 | cellular_component | branched-chain alpha-ketoacid dehydrogenase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 1401 |
| Chain | Residue |
| A | GLU193 |
| A | ASN222 |
| A | TYR224 |
| A | THV1403 |
| A | HOH2291 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1402 |
| Chain | Residue |
| A | HOH2078 |
| A | SER161 |
| A | PRO163 |
| A | THR166 |
| A | GLN167 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B 1343 |
| Chain | Residue |
| B | GLY128 |
| B | LEU130 |
| B | THR131 |
| B | CYS178 |
| B | ASP181 |
| B | ASN183 |
| B | HOH2136 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 1401 |
| Chain | Residue |
| C | GLU193 |
| C | ASN222 |
| C | TYR224 |
| C | THV1403 |
| C | HOH2297 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1402 |
| Chain | Residue |
| C | SER161 |
| C | PRO163 |
| C | THR166 |
| C | GLN167 |
| C | HOH2094 |
| C | HOH2096 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K D 1343 |
| Chain | Residue |
| D | GLY128 |
| D | LEU130 |
| D | THR131 |
| D | CYS178 |
| D | ASP181 |
| D | ASN183 |
| D | HOH2144 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE THV A 1403 |
| Chain | Residue |
| A | PHE85 |
| A | MET87 |
| A | GLN112 |
| A | TYR113 |
| A | ARG114 |
| A | SER162 |
| A | LEU164 |
| A | GLY192 |
| A | GLU193 |
| A | GLY194 |
| A | ALA195 |
| A | GLU198 |
| A | ARG220 |
| A | ASN222 |
| A | TYR224 |
| A | ALA225 |
| A | ILE226 |
| A | HIS291 |
| A | MN1401 |
| A | HOH2203 |
| D | GLU46 |
| D | LEU74 |
| D | GLU76 |
| D | GLN98 |
| D | TYR102 |
| D | HIS146 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE THV C 1403 |
| Chain | Residue |
| B | GLU46 |
| B | LEU74 |
| B | GLU76 |
| B | GLN98 |
| B | TYR102 |
| B | HIS146 |
| C | GLN112 |
| C | TYR113 |
| C | ARG114 |
| C | SER162 |
| C | LEU164 |
| C | GLY192 |
| C | GLU193 |
| C | GLY194 |
| C | ALA195 |
| C | GLU198 |
| C | ARG220 |
| C | ASN222 |
| C | TYR224 |
| C | ALA225 |
| C | ILE226 |
| C | HIS291 |
| C | MN1401 |
| C | HOH2217 |
| C | HOH2297 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1344 |
| Chain | Residue |
| A | GLN374 |
| B | TRP260 |
| B | GLU290 |
| B | THR294 |
| B | HOH2206 |
| B | HOH2243 |
| D | THR284 |
| D | ARG309 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 1344 |
| Chain | Residue |
| D | THR294 |
| D | HOH2236 |
| D | HOH2237 |
| B | THR284 |
| B | ARG309 |
| C | GLN374 |
| D | TRP260 |
| D | GLU290 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 1345 |
| Chain | Residue |
| C | GLN374 |
| D | SER211 |
| D | TRP260 |
| D | ASP261 |
| D | VAL262 |
| D | ASP263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10745006","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DTW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by BCKDK","evidences":[{"source":"PubMed","id":"19411760","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22589535","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P50136","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50136","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P50136","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q6P3A8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | HIS291 | |
| B | GLU76 | |
| B | HIS146 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | HIS291 | |
| D | GLU76 | |
| D | HIS146 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 280 |
| Chain | Residue | Details |
| A | GLU76 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
| A | SER162 | hydrogen bond acceptor, steric role |
| A | HIS291 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER292 | hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 280 |
| Chain | Residue | Details |
| C | GLU76 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
| C | SER162 | hydrogen bond acceptor, steric role |
| C | HIS291 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | SER292 | hydrogen bond acceptor, hydrogen bond donor |
