1DTW
HUMAN BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) 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 | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047101 | molecular_function | branched-chain alpha-keto acid dehydrogenase activity |
| A | 0160157 | cellular_component | branched-chain alpha-ketoacid dehydrogenase complex |
| B | 0003824 | molecular_function | catalytic activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU193 |
| A | ASN222 |
| A | TYR224 |
| A | TPP403 |
| A | HOH417 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 402 |
| Chain | Residue |
| A | SER161 |
| A | PRO163 |
| A | THR166 |
| A | GLN167 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B 343 |
| Chain | Residue |
| B | GLY128 |
| B | LEU130 |
| B | THR131 |
| B | CYS178 |
| B | ASP181 |
| B | ASN183 |
| B | HOH364 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP A 403 |
| Chain | Residue |
| A | GLN112 |
| A | TYR113 |
| A | ARG114 |
| A | SER162 |
| A | LEU164 |
| A | GLY192 |
| A | GLU193 |
| A | GLY194 |
| A | ALA195 |
| A | ARG220 |
| A | ASN222 |
| A | TYR224 |
| A | ALA225 |
| A | ILE226 |
| A | HIS291 |
| A | MG401 |
| A | HOH417 |
| B | GLU46 |
| B | LEU74 |
| B | GLU76 |
| B | GLN98 |
| B | TYR102 |
| B | HOH352 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW |
| Chain | Residue | Details |
| B | CYS178 | |
| B | ASP181 | |
| B | ASN183 | |
| A | GLU193 | |
| A | GLY194 | |
| A | ALA195 | |
| A | ARG220 | |
| A | ASN222 | |
| A | TYR224 | |
| A | HIS291 | |
| B | TYR102 | |
| B | GLY128 | |
| B | LEU130 | |
| B | THR131 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q6P3A8 |
| Chain | Residue | Details |
| B | LYS182 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| B | LYS191 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50136 |
| Chain | Residue | Details |
| A | SER302 | |
| A | SER294 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P50136 |
| Chain | Residue | Details |
| A | LYS311 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50136 |
| Chain | Residue | Details |
| A | LYS335 |
Catalytic Information from CSA
| 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 |
