2J5K
2.0 A resolution structure of the wild type malate dehydrogenase from Haloarcula marismortui (radiation damage series)
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 | 0005737 | cellular_component | cytoplasm | 
| 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 | 0005737 | cellular_component | cytoplasm | 
| 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 | 0005737 | cellular_component | cytoplasm | 
| 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 | 0005737 | cellular_component | cytoplasm | 
| 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 | 4 | 
| Details | BINDING SITE FOR RESIDUE CL A1331 | 
| Chain | Residue | 
| A | LYS205 | 
| A | ASP306 | 
| D | THR210 | 
| D | ASP211 | 
| site_id | AC2 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CL A1332 | 
| Chain | Residue | 
| A | THR210 | 
| A | ASP211 | 
| A | HOH2073 | 
| D | LYS205 | 
| D | ASP306 | 
| site_id | AC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CL A1333 | 
| Chain | Residue | 
| A | ARG166 | 
| A | ARG252 | 
| A | HIS256 | 
| B | ASP73 | 
| B | HOH2037 | 
| site_id | AC4 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE CL B1331 | 
| Chain | Residue | 
| B | LYS205 | 
| B | ASP306 | 
| C | THR210 | 
| C | ASP211 | 
| site_id | AC5 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CL B1332 | 
| Chain | Residue | 
| A | TYR72 | 
| A | ASP73 | 
| A | HOH2049 | 
| B | ARG166 | 
| B | ARG252 | 
| B | HIS256 | 
| site_id | AC6 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE CL C1331 | 
| Chain | Residue | 
| B | THR210 | 
| B | ASP211 | 
| C | LYS205 | 
| C | ASP306 | 
| site_id | AC7 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CL C1332 | 
| Chain | Residue | 
| C | ARG166 | 
| C | ARG252 | 
| C | HIS256 | 
| D | ASP73 | 
| D | HOH2058 | 
| site_id | AC8 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CL D1331 | 
| Chain | Residue | 
| C | ASP73 | 
| D | ARG166 | 
| D | ARG252 | 
| D | HIS256 | 
| D | HOH2208 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 4 | 
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 40 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12581646","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 14 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]} | 
| 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 | HIS195 | |
| A | ASP168 | 
| site_id | CSA2 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| B | HIS195 | |
| B | ASP168 | 
| site_id | CSA3 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| C | HIS195 | |
| C | ASP168 | 
| site_id | CSA4 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| D | HIS195 | |
| D | ASP168 | 
| site_id | CSA5 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| A | HIS195 | |
| A | ARG171 | |
| A | ASP168 | 
| site_id | CSA6 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| B | HIS195 | |
| B | ARG171 | |
| B | ASP168 | 
| site_id | CSA7 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| C | HIS195 | |
| C | ARG171 | |
| C | ASP168 | 
| site_id | CSA8 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1emd | 
| Chain | Residue | Details | 
| D | HIS195 | |
| D | ARG171 | |
| D | ASP168 | 






