6UOI
Crystal structure of cytosolic fumarate hydratase from Leishmania major in a complex with malonate
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 | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006106 | biological_process | fumarate metabolic process |
| A | 0006108 | biological_process | malate 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 | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006106 | biological_process | fumarate metabolic process |
| B | 0006108 | biological_process | malate 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 | 10 |
| Details | binding site for residue MLA A 601 |
| Chain | Residue |
| A | GLN134 |
| B | HIS334 |
| A | ASP135 |
| A | ARG173 |
| A | ARG421 |
| A | THR467 |
| A | THR468 |
| A | ARG471 |
| A | HOH705 |
| A | HOH746 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MLA A 602 |
| Chain | Residue |
| A | ILE140 |
| A | LEU142 |
| A | GLN195 |
| A | ASP197 |
| A | LYS271 |
| A | LYS274 |
| B | GLU267 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue MLA A 603 |
| Chain | Residue |
| A | PRO40 |
| A | HIS41 |
| A | HIS42 |
| A | PHE47 |
| A | LYS144 |
| A | GLU207 |
| A | PHE208 |
| A | LEU353 |
| A | ALA354 |
| A | HIS355 |
| A | HOH904 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | PRO37 |
| A | PRO40 |
| A | HIS42 |
| A | LYS144 |
| A | TYR280 |
| A | TYR281 |
| A | HOH949 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue F3S A 605 |
| Chain | Residue |
| A | CYS133 |
| A | GLN134 |
| A | GLY214 |
| A | ALA251 |
| A | CYS252 |
| A | CYS346 |
| A | ALA348 |
| A | LYS491 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue FE A 606 |
| Chain | Residue |
| A | ASN219 |
| A | THR468 |
| A | ARG471 |
| A | HOH815 |
| A | HOH1033 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue MLA B 601 |
| Chain | Residue |
| A | HIS334 |
| B | GLN134 |
| B | ASP135 |
| B | ARG173 |
| B | ARG421 |
| B | THR467 |
| B | THR468 |
| B | ARG471 |
| B | HOH726 |
| B | HOH764 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue MLA B 602 |
| Chain | Residue |
| A | GLU267 |
| B | ILE140 |
| B | LEU142 |
| B | GLN195 |
| B | ASP197 |
| B | LYS271 |
| B | LYS274 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue MLA B 603 |
| Chain | Residue |
| B | PRO40 |
| B | HIS41 |
| B | HIS42 |
| B | PHE47 |
| B | LYS144 |
| B | GLU207 |
| B | PHE208 |
| B | ALA354 |
| B | HIS355 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue F3S B 604 |
| Chain | Residue |
| B | CYS133 |
| B | GLN134 |
| B | GLY214 |
| B | ALA251 |
| B | CYS252 |
| B | CYS346 |
| B | ALA348 |
| B | LYS491 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 605 |
| Chain | Residue |
| B | ASN219 |
| B | THR468 |
| B | ARG471 |
| B | HOH811 |
| B | HOH1062 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27528683","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5L2R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
