6MSO
Crystal structure of mitochondrial fumarate hydratase from Leishmania major in a complex with inhibitor thiomalate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004333 | molecular_function | fumarate hydratase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
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 | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004333 | molecular_function | fumarate hydratase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
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 | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004333 | molecular_function | fumarate hydratase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0006091 | biological_process | generation of precursor metabolites and energy |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0006106 | biological_process | fumarate metabolic process |
C | 0006108 | biological_process | malate metabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016836 | molecular_function | hydro-lyase activity |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004333 | molecular_function | fumarate hydratase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0006091 | biological_process | generation of precursor metabolites and energy |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006106 | biological_process | fumarate metabolic process |
D | 0006108 | biological_process | malate metabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016836 | molecular_function | hydro-lyase activity |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue SF4 A 601 |
Chain | Residue |
A | CYS114 |
A | GLN115 |
A | GLY195 |
A | CYS233 |
A | CYS328 |
A | ALA330 |
A | LYS474 |
A | JYD608 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue GOL A 602 |
Chain | Residue |
A | TYR28 |
A | LYS337 |
A | HIS23 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue GOL A 603 |
Chain | Residue |
A | LYS288 |
A | GLN291 |
A | LYS302 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue GOL A 604 |
Chain | Residue |
A | LYS150 |
A | ARG151 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL A 605 |
Chain | Residue |
A | ARG278 |
A | ASP307 |
A | ARG309 |
A | HOH890 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue GOL A 606 |
Chain | Residue |
A | GLN438 |
A | HOH878 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue 1PE A 607 |
Chain | Residue |
A | LEU30 |
A | LYS33 |
A | ASP341 |
A | TRP344 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue JYD A 608 |
Chain | Residue |
A | GLN115 |
A | ASP116 |
A | ARG154 |
A | GLY196 |
A | GLY197 |
A | ARG404 |
A | THR450 |
A | THR451 |
A | ARG454 |
A | LYS474 |
A | SF4601 |
A | HOH826 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue 1PE A 609 |
Chain | Residue |
A | GLN354 |
B | GLN354 |
B | TYR355 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue 1PE A 610 |
Chain | Residue |
A | ALA409 |
A | ARG412 |
A | GLU413 |
A | GLU416 |
A | HOH827 |
B | ASN213 |
B | SER216 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue 1PE A 611 |
Chain | Residue |
A | GLN463 |
A | GLY466 |
A | TYR488 |
A | HOH892 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue SF4 B 601 |
Chain | Residue |
B | CYS114 |
B | GLN115 |
B | GLY195 |
B | CYS233 |
B | CYS328 |
B | ALA330 |
B | LYS474 |
B | JYD604 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GOL B 602 |
Chain | Residue |
B | HIS23 |
B | TYR28 |
B | LYS337 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue GOL B 603 |
Chain | Residue |
B | GLY520 |
B | MET521 |
B | HOH816 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue JYD B 604 |
Chain | Residue |
B | GLN115 |
B | ASP116 |
B | ARG154 |
B | GLY196 |
B | GLY197 |
B | ARG404 |
B | THR450 |
B | THR451 |
B | ARG454 |
B | LYS474 |
B | SF4601 |
B | HOH717 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue 1PE B 605 |
Chain | Residue |
B | LYS33 |
B | ASP341 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue 1PE B 606 |
Chain | Residue |
B | GLU87 |
B | GLN291 |
B | LYS302 |
B | HOH774 |
B | HOH793 |
B | HOH794 |
site_id | AD9 |
Number of Residues | 9 |
Details | binding site for residue SF4 C 601 |
Chain | Residue |
C | CYS114 |
C | GLN115 |
C | GLY195 |
C | ALA232 |
C | CYS233 |
C | CYS328 |
C | ALA330 |
C | LYS474 |
C | JYD604 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue GOL C 602 |
Chain | Residue |
D | HOH775 |
C | LYS215 |
C | SER216 |
C | ASN219 |
C | HOH802 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue 1PE C 603 |
Chain | Residue |
C | GLN354 |
D | ARG80 |
site_id | AE3 |
Number of Residues | 12 |
Details | binding site for residue JYD C 604 |
Chain | Residue |
C | GLN115 |
C | ASP116 |
C | ARG154 |
C | GLY196 |
C | GLY197 |
C | ARG404 |
C | THR450 |
C | THR451 |
C | ARG454 |
C | LYS474 |
C | SF4601 |
C | HOH718 |
site_id | AE4 |
Number of Residues | 6 |
Details | binding site for residue 1PE C 605 |
Chain | Residue |
C | GLU87 |
C | GLU284 |
C | LYS288 |
C | GLN291 |
C | LYS302 |
C | HOH764 |
site_id | AE5 |
Number of Residues | 7 |
Details | binding site for residue 1PE C 606 |
Chain | Residue |
C | SER78 |
C | LYS81 |
C | TYR303 |
C | HIS306 |
C | ASP307 |
C | ARG309 |
C | HOH764 |
site_id | AE6 |
Number of Residues | 8 |
Details | binding site for residue SF4 D 601 |
Chain | Residue |
D | CYS114 |
D | GLN115 |
D | ALA232 |
D | CYS233 |
D | CYS328 |
D | ALA330 |
D | LYS474 |
D | JYD602 |
site_id | AE7 |
Number of Residues | 10 |
Details | binding site for residue JYD D 602 |
Chain | Residue |
D | GLN115 |
D | ASP116 |
D | ARG154 |
D | GLY197 |
D | ARG404 |
D | THR450 |
D | THR451 |
D | ARG454 |
D | LYS474 |
D | SF4601 |
site_id | AE8 |
Number of Residues | 4 |
Details | binding site for residue 1PE D 603 |
Chain | Residue |
B | LYS487 |
B | TYR488 |
D | LYS33 |
D | ASP341 |
Functional Information from PROSITE/UniProt
site_id | PS00163 |
Number of Residues | 10 |
Details | FUMARATE_LYASES Fumarate lyases signature. GSmvMlAKgN |
Chain | Residue | Details |
A | GLY467-ASN476 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO |
Chain | Residue | Details |
A | CYS114 | |
D | CYS114 | |
D | CYS233 | |
D | CYS328 | |
A | CYS233 | |
A | CYS328 | |
B | CYS114 | |
B | CYS233 | |
B | CYS328 | |
C | CYS114 | |
C | CYS233 | |
C | CYS328 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:E9AE57 |
Chain | Residue | Details |
A | GLN115 | |
B | GLY197 | |
B | ASN200 | |
B | ARG404 | |
B | THR450 | |
B | LYS474 | |
C | GLN115 | |
C | ARG154 | |
C | GLY197 | |
C | ASN200 | |
C | ARG404 | |
A | ARG154 | |
C | THR450 | |
C | LYS474 | |
D | GLN115 | |
D | ARG154 | |
D | GLY197 | |
D | ASN200 | |
D | ARG404 | |
D | THR450 | |
D | LYS474 | |
A | GLY197 | |
A | ASN200 | |
A | ARG404 | |
A | THR450 | |
A | LYS474 | |
B | GLN115 | |
B | ARG154 |