1LLQ
Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 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 | 0003824 | molecular_function | catalytic activity |
| 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 | 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 | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12853453","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12853453","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O0S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P23368","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12033925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12853453","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LLQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O0S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12033925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12853453","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LLQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O0S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
