1SEV
Mature and translocatable forms of glyoxysomal malate dehydrogenase have different activities and stabilities but similar crystal structures
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006108 | biological_process | malate metabolic process |
A | 0009514 | cellular_component | glyoxysome |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016615 | molecular_function | malate dehydrogenase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006108 | biological_process | malate metabolic process |
B | 0009514 | cellular_component | glyoxysome |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016615 | molecular_function | malate dehydrogenase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
Functional Information from PROSITE/UniProt
site_id | PS00068 |
Number of Residues | 13 |
Details | MDH Malate dehydrogenase active site signature. VTMLDvvRAntfV |
Chain | Residue | Details |
A | VAL189-VAL201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS220 | |
B | HIS220 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY51 | |
B | MET271 | |
A | ASP77 | |
A | ASN137 | |
A | ILE160 | |
A | MET271 | |
B | GLY51 | |
B | ASP77 | |
B | ASN137 | |
B | ILE160 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG124 | |
A | ARG130 | |
A | ASN162 | |
A | ARG196 | |
B | ARG124 | |
B | ARG130 | |
B | ASN162 | |
B | ARG196 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | ASP193 | |
A | HIS220 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | ASP193 | |
B | HIS220 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | ASP193 | |
A | HIS220 | |
A | ARG196 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | ASP193 | |
B | HIS220 | |
B | ARG196 |