6NTE
Crystal Structure of Synechocystis Dihydroxyacid Dehydratase (DHAD)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
| 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 | valine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | valine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PROSITE/UniProt
| site_id | PS00886 |
| Number of Residues | 11 |
| Details | ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKnmPGamiA |
| Chain | Residue | Details |
| A | CYS123-ALA133 |
| site_id | PS00887 |
| Number of Residues | 12 |
| Details | ILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. GLITDGRFSGGT |
| Chain | Residue | Details |
| A | GLY465-THR476 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00012 |
| Chain | Residue | Details |
| A | SER473 | |
| B | SER473 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00012 |
| Chain | Residue | Details |
| A | CYS50 | |
| B | CYS50 | |
| B | ASP82 | |
| B | CYS123 | |
| B | ASP124 | |
| B | CYS195 | |
| B | GLU447 | |
| A | ASP82 | |
| A | CYS123 | |
| A | ASP124 | |
| A | CYS195 | |
| A | GLU447 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00012 |
| Chain | Residue | Details |
| A | LYS125 | |
| B | LYS125 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00012 |
| Chain | Residue | Details |
| A | LYS125 | |
| B | LYS125 |
