6UOJ
Crystal structure of cytosolic fumarate hydratase from Leishmania major in a complex with succinate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004333 | molecular_function | fumarate hydratase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0006106 | biological_process | fumarate metabolic process |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0020015 | cellular_component | glycosome |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0097014 | cellular_component | ciliary plasm |
| B | 0004333 | molecular_function | fumarate hydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0006106 | biological_process | fumarate metabolic process |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0008152 | biological_process | metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0020015 | cellular_component | glycosome |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0097014 | cellular_component | ciliary plasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 A 601 |
| Chain | Residue |
| A | CYS133 |
| A | ASP135 |
| A | GLY214 |
| A | ALA251 |
| A | CYS252 |
| A | CYS346 |
| A | ALA348 |
| A | SIN602 |
| A | HOH708 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue SIN A 602 |
| Chain | Residue |
| A | GLN134 |
| A | ASP135 |
| A | ARG173 |
| A | GLY216 |
| A | ARG421 |
| A | THR467 |
| A | THR468 |
| A | ARG471 |
| A | LYS491 |
| A | SF4601 |
| A | HOH708 |
| A | HOH719 |
| B | ALA336 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 601 |
| Chain | Residue |
| B | CYS133 |
| B | GLN134 |
| B | GLY214 |
| B | CYS252 |
| B | CYS346 |
| B | ALA348 |
| B | LYS491 |
| B | SIN602 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue SIN B 602 |
| Chain | Residue |
| A | HIS334 |
| B | GLN134 |
| B | ASP135 |
| B | ARG173 |
| B | GLY216 |
| B | ARG421 |
| B | THR467 |
| B | THR468 |
| B | ARG471 |
| B | LYS491 |
| B | SF4601 |
| B | HOH758 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| B | LYS55 |
| B | ASN71 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 604 |
| Chain | Residue |
| A | ARG65 |
| B | VAL70 |
| B | PRO72 |
| B | TRP150 |
| B | THR151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R |
| Chain | Residue | Details |
| A | CYS133 | |
| A | LYS491 | |
| B | CYS133 | |
| B | GLN134 | |
| B | ARG173 | |
| B | GLY216 | |
| B | ASN219 | |
| B | CYS252 | |
| B | CYS346 | |
| B | ARG421 | |
| B | THR467 | |
| A | GLN134 | |
| B | LYS491 | |
| A | ARG173 | |
| A | GLY216 | |
| A | ASN219 | |
| A | CYS252 | |
| A | CYS346 | |
| A | ARG421 | |
| A | THR467 |
