6UPO
Crystal structure of H334A 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 | 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 | 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 | 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 | 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 | ASP135 |
A | GLY214 |
A | ALA251 |
A | CYS252 |
A | CYS346 |
A | ALA348 |
A | LMR602 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue LMR A 602 |
Chain | Residue |
A | ASP135 |
A | ARG173 |
A | GLY215 |
A | GLY216 |
A | ARG421 |
A | THR467 |
A | THR468 |
A | ARG471 |
A | LYS491 |
A | SF4601 |
A | GLN134 |
site_id | AC3 |
Number of Residues | 8 |
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 | LMR602 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue LMR B 602 |
Chain | Residue |
A | ALA336 |
B | GLN134 |
B | ASP135 |
B | ARG173 |
B | GLY215 |
B | GLY216 |
B | ARG421 |
B | THR467 |
B | THR468 |
B | ARG471 |
B | LYS491 |
B | SF4601 |
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 |