6UPM
Crystal structure of T467A variant of cytosolic fumarate hydratase from Leishmania major in a complex with S-malate
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 | 8 |
| Details | binding site for residue SF4 A 601 |
| Chain | Residue |
| A | CYS133 |
| A | GLN134 |
| A | GLY214 |
| A | CYS252 |
| A | CYS346 |
| A | ALA348 |
| A | LYS491 |
| A | LMR602 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue LMR A 602 |
| Chain | Residue |
| A | ASP135 |
| A | ARG173 |
| A | GLY216 |
| A | ARG421 |
| A | THR468 |
| A | ARG471 |
| A | LYS491 |
| A | SF4601 |
| A | HOH841 |
| A | GLN134 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | ASN219 |
| A | LYS220 |
| A | TYR222 |
| A | ARG471 |
| A | HOH735 |
| A | HOH887 |
| A | HOH972 |
| B | GLN225 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 B 601 |
| Chain | Residue |
| B | CYS133 |
| B | GLN134 |
| B | ASP135 |
| B | GLY214 |
| B | CYS252 |
| B | CYS346 |
| B | ALA348 |
| B | LYS491 |
| B | LMR602 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue LMR B 602 |
| Chain | Residue |
| B | GLN134 |
| B | ASP135 |
| B | ARG173 |
| B | GLY215 |
| B | GLY216 |
| B | ARG421 |
| B | ALA467 |
| B | THR468 |
| B | ARG471 |
| B | LYS491 |
| B | SF4601 |
| B | HOH748 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| A | GLN225 |
| B | ASN219 |
| B | LYS220 |
| B | TYR222 |
| B | ARG471 |
| B | HOH769 |
| B | HOH953 |
| B | HOH989 |
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 |
