1LDN
STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION
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 | 0006096 | biological_process | glycolytic process |
| 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 | 0051287 | molecular_function | NAD binding |
| 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 | 0006096 | biological_process | glycolytic process |
| 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 | 0051287 | molecular_function | NAD binding |
| 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 | 0006096 | biological_process | glycolytic process |
| 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 | 0051287 | molecular_function | NAD binding |
| 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 | 0006096 | biological_process | glycolytic process |
| 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 | 0051287 | molecular_function | NAD binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006089 | biological_process | lactate metabolic process |
| E | 0006096 | biological_process | glycolytic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0019752 | biological_process | carboxylic acid metabolic process |
| E | 0051287 | molecular_function | NAD binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006089 | biological_process | lactate metabolic process |
| F | 0006096 | biological_process | glycolytic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0019752 | biological_process | carboxylic acid metabolic process |
| F | 0051287 | molecular_function | NAD binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006089 | biological_process | lactate metabolic process |
| G | 0006096 | biological_process | glycolytic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0019752 | biological_process | carboxylic acid metabolic process |
| G | 0051287 | molecular_function | NAD binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006089 | biological_process | lactate metabolic process |
| H | 0006096 | biological_process | glycolytic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0019752 | biological_process | carboxylic acid metabolic process |
| H | 0051287 | molecular_function | NAD binding |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. IGEHGDT |
| Chain | Residue | Details |
| A | ILE190-THR196 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 64 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","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 | ASP166 | |
| A | HIS193 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS193 | |
| B | ASP166 | |
| B | ARG169 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS193 | |
| C | ASP166 | |
| C | ARG169 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS193 | |
| D | ASP166 | |
| D | ARG169 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| E | HIS193 | |
| E | ASP166 | |
| E | ARG169 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| F | HIS193 | |
| F | ASP166 | |
| F | ARG169 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| G | HIS193 | |
| G | ASP166 | |
| G | ARG169 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| H | HIS193 | |
| H | ASP166 | |
| H | ARG169 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ASP166 | |
| B | HIS193 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ASP166 | |
| C | HIS193 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ASP166 | |
| D | HIS193 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| E | ASP166 | |
| E | HIS193 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| F | ASP166 | |
| F | HIS193 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| G | ASP166 | |
| G | HIS193 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| H | ASP166 | |
| H | HIS193 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS193 | |
| A | ASP166 | |
| A | ARG169 |
