4BGV
1.8 A resolution structure of the malate dehydrogenase from Picrophilus torridus in its apo form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030060 | molecular_function | L-malate dehydrogenase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030060 | molecular_function | L-malate dehydrogenase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006090 | biological_process | pyruvate metabolic process |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030060 | molecular_function | L-malate dehydrogenase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006090 | biological_process | pyruvate metabolic process |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030060 | molecular_function | L-malate dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 1325 |
| Chain | Residue |
| A | ALA13 |
| A | GLY229 |
| A | SER230 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 1326 |
| Chain | Residue |
| A | ILE24 |
| A | HOH2334 |
| A | HOH2335 |
| A | HOH2336 |
| B | ILE24 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT B 1325 |
| Chain | Residue |
| B | GLY62 |
| B | PHE63 |
| B | LYS70 |
| B | HOH2054 |
| B | HOH2072 |
| B | HOH2073 |
| B | HOH2323 |
| C | ASP95 |
| C | ILE315 |
| B | GLU41 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 1326 |
| Chain | Residue |
| B | TYR226 |
| B | GLY229 |
| B | SER230 |
| B | HOH2257 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 1327 |
| Chain | Residue |
| A | PHE232 |
| A | HOH2056 |
| A | HOH2269 |
| B | PHE232 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 1328 |
| Chain | Residue |
| B | GLU165 |
| B | LEU202 |
| B | LEU203 |
| B | PRO204 |
| B | HOH2324 |
| C | GLU300 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 1325 |
| Chain | Residue |
| A | ASP201 |
| A | LEU203 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG6 C 1326 |
| Chain | Residue |
| B | PRO198 |
| B | ASP201 |
| B | HOH2215 |
| B | HOH2233 |
| C | ARG190 |
| C | LYS293 |
| C | ASN295 |
| C | HOH2223 |
| C | HOH2305 |
| C | HOH2330 |
| C | HOH2330 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG C 1327 |
| Chain | Residue |
| C | ALA13 |
| C | GLY229 |
| C | SER230 |
| C | PHE232 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG C 1328 |
| Chain | Residue |
| A | HOH2335 |
| C | ILE24 |
| C | HOH2027 |
| C | HOH2331 |
| C | HOH2333 |
| D | ILE24 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG D 1325 |
| Chain | Residue |
| C | LYS43 |
| C | PHE232 |
| C | HOH2058 |
| C | HOH2271 |
| D | PHE232 |
| D | PEG1326 |
| D | HOH2224 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG D 1326 |
| Chain | Residue |
| D | TYR226 |
| D | GLY229 |
| D | SER230 |
| D | PEG1325 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG D 1327 |
| Chain | Residue |
| C | ALA66 |
| D | HOH2155 |
| D | HOH2160 |
| D | HOH2225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889 |
| Chain | Residue | Details |
| A | HIS181 | |
| B | HIS181 | |
| C | HIS181 | |
| D | HIS181 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O08349 |
| Chain | Residue | Details |
| B | GLY10 | |
| B | ASP34 | |
| B | ASN101 | |
| B | VAL124 | |
| C | GLY10 | |
| C | ASP34 | |
| C | ASN101 | |
| C | VAL124 | |
| D | GLY10 | |
| D | ASP34 | |
| D | ASN101 | |
| D | VAL124 | |
| A | GLY10 | |
| A | ASP34 | |
| A | ASN101 | |
| A | VAL124 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889 |
| Chain | Residue | Details |
| C | ARG88 | |
| C | ARG94 | |
| C | ASN126 | |
| C | ARG157 | |
| D | ARG88 | |
| D | ARG94 | |
| D | ASN126 | |
| D | ARG157 | |
| A | ARG88 | |
| A | ARG94 | |
| A | ARG157 | |
| B | ARG88 | |
| B | ARG94 | |
| B | ASN126 | |
| B | ARG157 | |
| A | ASN126 |
