1LLQ
Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004470 | molecular_function | malic enzyme activity |
A | 0004471 | molecular_function | malate dehydrogenase (decarboxylating) (NAD+) activity |
A | 0004473 | molecular_function | malate dehydrogenase (decarboxylating) (NADP+) activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006090 | biological_process | pyruvate metabolic process |
A | 0006108 | biological_process | malate metabolic process |
A | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0046872 | molecular_function | metal ion binding |
A | 0051287 | molecular_function | NAD binding |
B | 0004470 | molecular_function | malic enzyme activity |
B | 0004471 | molecular_function | malate dehydrogenase (decarboxylating) (NAD+) activity |
B | 0004473 | molecular_function | malate dehydrogenase (decarboxylating) (NADP+) activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006090 | biological_process | pyruvate metabolic process |
B | 0006108 | biological_process | malate metabolic process |
B | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0046872 | molecular_function | metal ion binding |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD A 1001 |
Chain | Residue |
A | ASN275 |
A | ILE362 |
A | ALA405 |
A | SER406 |
A | VAL408 |
A | LEU432 |
A | SER433 |
A | ASN434 |
A | GLY459 |
A | GLY477 |
A | ASN479 |
A | THR299 |
A | HOH2013 |
A | PHE326 |
A | GLY327 |
A | ALA328 |
A | GLY329 |
A | ALA330 |
A | ALA331 |
A | ASP361 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD B 1002 |
Chain | Residue |
B | ASN275 |
B | THR299 |
B | PHE326 |
B | ALA328 |
B | GLY329 |
B | ALA330 |
B | ALA331 |
B | ASP361 |
B | ILE362 |
B | ALA405 |
B | SER406 |
B | VAL408 |
B | LEU432 |
B | SER433 |
B | ASN434 |
B | GLY459 |
B | GLY477 |
B | ASN479 |
Functional Information from PROSITE/UniProt
site_id | PS00331 |
Number of Residues | 17 |
Details | MALIC_ENZYMES Malic enzymes signature. FnDDiqGTAsViVAGLL |
Chain | Residue | Details |
A | PHE292-LEU308 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | TYR126 | |
B | TYR126 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS199 | |
B | LYS199 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12853453 |
Chain | Residue | Details |
A | GLN78 | |
A | ARG81 | |
A | ARG105 | |
B | GLN78 | |
B | ARG81 | |
B | ARG105 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12033925, ECO:0000269|PubMed:12853453 |
Chain | Residue | Details |
A | ARG181 | |
A | ASP295 | |
A | GLY327 | |
A | ASN434 | |
B | ARG181 | |
B | ASP295 | |
B | GLY327 | |
B | ASN434 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU271 | |
A | ASP272 | |
B | GLU271 | |
B | ASP272 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Important for activity |
Chain | Residue | Details |
A | ASP295 | |
B | ASP295 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1do8 |
Chain | Residue | Details |
A | LYS199 | |
A | TYR126 | |
A | ASP294 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1do8 |
Chain | Residue | Details |
B | LYS199 | |
B | TYR126 | |
B | ASP294 |