1LLC
STRUCTURE DETERMINATION OF THE ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS CASEI AT 3.0 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 |
Functional Information from PDB Data
| site_id | AFP |
| Number of Residues | 7 |
| Details | RESIDUES CLOSE TO THE MOLECULAR P AXIS THAT BIND THE ALLOSTERIC ACTIVATOR |
| Chain | Residue |
| A | THR169 |
| A | ARG173 |
| A | HIS188 |
| A | TYR190 |
| A | ARG256 |
| A | VAL268 |
| A | LEU269 |
| site_id | SO4 |
| Number of Residues | 3 |
| Details | RESIDUES BINDING THE SULFATE |
| Chain | Residue |
| A | THR246 |
| A | ARG171 |
| A | HIS195 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. MGEHGDT |
| Chain | Residue | Details |
| A | MET192-THR198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"1984","firstPage":"32","lastPage":"34","volume":"40","journal":"Acta Crystallogr. A","title":"Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution.","authors":["Buehner M.","Hecht H.J."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"1LLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| 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 | HIS195 | |
| A | ASP168 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ARG171 | |
| A | ASP168 |
