3GVH
Crystal structure of Lactate/malate dehydrogenase from Brucella melitensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0006089 | biological_process | lactate 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 (NAD+) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| B | 0006089 | biological_process | lactate 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 (NAD+) activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| C | 0006089 | biological_process | lactate 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 (NAD+) activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| D | 0006089 | biological_process | lactate 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 (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | GLY12 |
| A | GLN102 |
| A | ILE119 |
| A | ASN121 |
| A | MET144 |
| A | LEU148 |
| A | HIS176 |
| A | HOH330 |
| A | HOH427 |
| A | HOH503 |
| A | MET13 |
| A | ILE14 |
| A | ASP34 |
| A | ILE35 |
| A | THR78 |
| A | ALA79 |
| A | GLY80 |
| A | VAL99 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD B 400 |
| Chain | Residue |
| B | GLY12 |
| B | MET13 |
| B | ILE14 |
| B | PHE33 |
| B | ASP34 |
| B | ILE35 |
| B | THR78 |
| B | ILE119 |
| B | ASN121 |
| B | MET144 |
| B | LEU148 |
| B | HIS176 |
| B | HOH351 |
| B | HOH413 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD C 400 |
| Chain | Residue |
| C | GLY12 |
| C | MET13 |
| C | ILE14 |
| C | ASP34 |
| C | ILE35 |
| C | THR78 |
| C | GLY80 |
| C | ILE119 |
| C | ASN121 |
| C | LEU123 |
| C | MET144 |
| C | HIS176 |
| C | HOH376 |
| C | HOH404 |
| C | HOH405 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD D 400 |
| Chain | Residue |
| D | GLY12 |
| D | MET13 |
| D | ILE14 |
| D | ASP34 |
| D | THR78 |
| D | ALA79 |
| D | VAL99 |
| D | ILE119 |
| D | ASN121 |
| D | MET144 |
| D | LEU148 |
| D | HIS176 |
| D | HOH351 |
| D | HOH378 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 49 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ASP149 | |
| A | HIS176 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ASP149 | |
| B | HIS176 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ASP149 | |
| C | HIS176 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ASP149 | |
| D | HIS176 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ARG152 | |
| A | ASP149 | |
| A | HIS176 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ARG152 | |
| B | ASP149 | |
| B | HIS176 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ARG152 | |
| C | ASP149 | |
| C | HIS176 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ARG152 | |
| D | ASP149 | |
| D | HIS176 |
