Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009536 | cellular_component | plastid |
| A | 0009553 | biological_process | embryo sac development |
| A | 0009555 | biological_process | pollen development |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0009651 | biological_process | response to salt stress |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048364 | biological_process | root development |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 601 |
| Chain | Residue |
| A | CYS66 |
| A | ASP98 |
| A | ALA99 |
| A | CYS139 |
| A | ASP140 |
| A | CYS211 |
| A | ALA217 |
| A | ACT605 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | THR104 |
| A | ARG105 |
| A | TRP129 |
| A | ARG25 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | ASN17 |
| A | PRO29 |
| A | LYS30 |
| A | SER31 |
| A | TYR184 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | SER45 |
| A | ASP46 |
| A | HIS202 |
| A | HOH804 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 605 |
| Chain | Residue |
| A | CYS211 |
| A | TYR215 |
| A | FES601 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 606 |
| Chain | Residue |
| A | ASP98 |
| A | ASP140 |
| A | LYS141 |
| A | GLU463 |
Functional Information from PROSITE/UniProt
| site_id | PS00886 |
| Number of Residues | 11 |
| Details | ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKnmPGtimA |
| Chain | Residue | Details |
| A | CYS139-ALA149 | |
| site_id | PS00887 |
| Number of Residues | 12 |
| Details | ILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. ALLTDGRFSGGS |
| Chain | Residue | Details |
| A | ALA481-SER492 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P9WKJ5","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29995859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZE4","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WKJ5","evidenceCode":"ECO:0000250"}]} |
