1UM9
branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 in apo-form
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 | 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 | 0003863 | molecular_function | branched-chain 2-oxo acid dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0003863 | molecular_function | branched-chain 2-oxo acid dehydrogenase 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 | 0003863 | molecular_function | branched-chain 2-oxo acid dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1402 |
| Chain | Residue |
| A | TYR94 |
| A | TYR95 |
| A | ARG96 |
| A | GLY174 |
| A | ARG269 |
| A | HIS273 |
| A | HOH1458 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2402 |
| Chain | Residue |
| C | ARG96 |
| C | GLY174 |
| C | HIS273 |
| C | HOH2462 |
| C | HOH2465 |
| C | HOH2607 |
| C | TYR94 |
| C | TYR95 |
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 | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15033367","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| 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 | 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 |
