Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00886 |
| Number of Residues | 11 |
| Details | ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKnmPGvlmA |
| Chain | Residue | Details |
| A | CYS159-ALA169 | |
| site_id | PS00887 |
| Number of Residues | 12 |
| Details | ILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. ALLTDGRFSGGS |
| Chain | Residue | Details |
| A | ALA503-SER514 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P9WKJ5","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WKJ5","evidenceCode":"ECO:0000250"}]} |