1UMB
branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 in holo-form
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 | 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 | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0007584 | biological_process | response to nutrient |
| B | 0009083 | biological_process | branched-chain amino acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
| C | 0005515 | molecular_function | protein binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0007584 | biological_process | response to nutrient |
| D | 0009083 | biological_process | branched-chain amino acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1401 |
| Chain | Residue |
| A | ASP175 |
| A | ASN204 |
| A | TYR206 |
| A | TPP1402 |
| A | HOH1423 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2401 |
| Chain | Residue |
| C | HOH2416 |
| C | ASP175 |
| C | ASN204 |
| C | TYR206 |
| C | TPP2402 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP A 1402 |
| Chain | Residue |
| A | TYR94 |
| A | TYR95 |
| A | ARG96 |
| A | SER144 |
| A | PRO145 |
| A | ILE146 |
| A | GLY174 |
| A | ASP175 |
| A | GLY176 |
| A | ALA177 |
| A | GLU180 |
| A | ASN204 |
| A | TYR206 |
| A | ALA207 |
| A | ILE208 |
| A | HIS273 |
| A | MG1401 |
| A | HOH1404 |
| A | HOH1423 |
| A | HOH1433 |
| D | GLU29 |
| D | LEU58 |
| D | GLU60 |
| D | GLN82 |
| D | TYR86 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP C 2402 |
| Chain | Residue |
| B | GLU29 |
| B | LEU58 |
| B | GLU60 |
| B | GLN82 |
| B | TYR86 |
| C | TYR94 |
| C | TYR95 |
| C | ARG96 |
| C | SER144 |
| C | PRO145 |
| C | ILE146 |
| C | GLY174 |
| C | ASP175 |
| C | GLY176 |
| C | ALA177 |
| C | GLU180 |
| C | ASN204 |
| C | TYR206 |
| C | ALA207 |
| C | ILE208 |
| C | HIS273 |
| C | MG2401 |
| C | HOH2416 |
| C | HOH2422 |
| C | HOH2452 |
Functional Information from PROSITE/UniProt
| site_id | PS00014 |
| Number of Residues | 4 |
| Details | ER_TARGET Endoplasmic reticulum targeting sequence. KEEL |
| Chain | Residue | Details |
| A | LYS364-LEU367 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305 |
| Chain | Residue | Details |
| B | HIS129 | |
| A | HIS273 | |
| C | PHE66 | |
| C | TYR94 | |
| C | TYR95 | |
| C | MET128 | |
| C | SER144 | |
| C | GLY174 | |
| C | ASP175 | |
| C | ASN204 | |
| C | TYR206 | |
| D | HIS129 | |
| C | HIS273 | |
| A | TYR95 | |
| A | MET128 | |
| A | SER144 | |
| A | GLY174 | |
| A | ASP175 | |
| A | ASN204 | |
| A | TYR206 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15033367 |
| Chain | Residue | Details |
| B | GLU29 | |
| B | GLN82 | |
| D | GLU29 | |
| D | GLN82 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | LEU58 | |
| B | PHE83 | |
| B | TYR86 | |
| D | LEU58 | |
| D | PHE83 | |
| D | TYR86 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| B | HIS129 | |
| D | HIS129 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | HIS273 | |
| B | GLU60 | |
| B | HIS129 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | HIS273 | |
| D | GLU60 | |
| D | HIS129 |
