2E37
Structure of TT0471 protein from Thermus thermophilus
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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1501 |
| Chain | Residue |
| B | VAL6 |
| B | GLY7 |
| B | ASP32 |
| B | LEU33 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 H 1502 |
| Chain | Residue |
| H | ASP32 |
| H | LEU33 |
| H | TYR62 |
| H | ALA75 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD A 1401 |
| Chain | Residue |
| A | GLY9 |
| A | MSE10 |
| A | VAL11 |
| A | ASP32 |
| A | LEU33 |
| A | LEU37 |
| A | ALA74 |
| A | ALA75 |
| A | GLY76 |
| A | VAL77 |
| A | ASN92 |
| A | THR116 |
| A | ASN117 |
| A | ILE221 |
| A | ALA226 |
| A | THR227 |
| A | HOH1411 |
| A | SER8 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD C 1402 |
| Chain | Residue |
| C | GLY7 |
| C | SER8 |
| C | GLY9 |
| C | MSE10 |
| C | VAL11 |
| C | ASP32 |
| C | LEU33 |
| C | LEU37 |
| C | ALA75 |
| C | GLY76 |
| C | VAL77 |
| C | ASN92 |
| C | VAL95 |
| C | ASN117 |
| C | ILE221 |
| C | ALA226 |
| C | THR227 |
| C | HOH1479 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD E 1403 |
| Chain | Residue |
| E | SER8 |
| E | GLY9 |
| E | MSE10 |
| E | VAL11 |
| E | ASP32 |
| E | LEU33 |
| E | LEU37 |
| E | ALA75 |
| E | GLY76 |
| E | VAL77 |
| E | ASN92 |
| E | ASN117 |
| E | ILE221 |
| E | ALA226 |
| E | THR227 |
| E | HOH1410 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD G 1404 |
| Chain | Residue |
| G | SER8 |
| G | GLY9 |
| G | MSE10 |
| G | VAL11 |
| G | ASP32 |
| G | LEU33 |
| G | LEU37 |
| G | ALA75 |
| G | GLY76 |
| G | VAL77 |
| G | ASN92 |
| G | VAL95 |
| G | ASN117 |
| G | ILE221 |
| G | ALA226 |
| G | THR227 |
| G | HOH1437 |
| G | HOH1480 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
| Chain | Residue | Details |
| A | LEU169-SER175 |
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":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Structure of TT0471 protein from Thermus thermophilus.","authors":["Lokanath N.K.","Kunishima N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PubMed","id":"22319152","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2E37","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZZN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| 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 | HIS172 | |
| A | ASP145 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS172 | |
| B | ASP145 | |
| B | ARG148 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS172 | |
| C | ASP145 | |
| C | ARG148 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS172 | |
| D | ASP145 | |
| D | ARG148 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| E | HIS172 | |
| E | ASP145 | |
| E | ARG148 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| F | HIS172 | |
| F | ASP145 | |
| F | ARG148 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| G | HIS172 | |
| G | ASP145 | |
| G | ARG148 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| H | HIS172 | |
| H | ASP145 | |
| H | ARG148 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS172 | |
| B | ASP145 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS172 | |
| C | ASP145 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS172 | |
| D | ASP145 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| E | HIS172 | |
| E | ASP145 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| F | HIS172 | |
| F | ASP145 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| G | HIS172 | |
| G | ASP145 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| H | HIS172 | |
| H | ASP145 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS172 | |
| A | ASP145 | |
| A | ARG148 |
