2V6M
Crystal structure of lactate dehydrogenase from Thermus Thermophilus HB8 (Apo form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 activity |
| D | 0005737 | cellular_component | cytoplasm |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES D1332 |
| Chain | Residue |
| C | PRO71 |
| D | ARG256 |
| D | TYR269 |
| D | HOH1025 |
| D | HOH1042 |
| D | HOH1088 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES B1332 |
| Chain | Residue |
| B | ARG256 |
| B | HOH1092 |
| B | HOH1146 |
| B | HOH1147 |
| A | PRO71 |
| A | PHE72 |
| B | ALA170 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MES C1332 |
| Chain | Residue |
| B | HOH1058 |
| C | ARG256 |
| D | PRO71 |
| D | PHE72 |
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 | LEU192-SER198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | HIS195 | |
| B | HIS195 | |
| C | HIS195 | |
| D | HIS195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.2, ECO:0000269|Ref.4, ECO:0000305|PubMed:22319152, ECO:0007744|PDB:2E37, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ, ECO:0007744|PDB:3ZZN |
| Chain | Residue | Details |
| A | MET31 | |
| D | MET31 | |
| D | ASP53 | |
| D | GLY99 | |
| A | ASP53 | |
| A | GLY99 | |
| B | MET31 | |
| B | ASP53 | |
| B | GLY99 | |
| C | MET31 | |
| C | ASP53 | |
| C | GLY99 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | TYR85 | |
| B | TYR85 | |
| C | TYR85 | |
| D | TYR85 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | GLN102 | |
| A | ASP168 | |
| B | GLN102 | |
| B | ASP168 | |
| C | GLN102 | |
| C | ASP168 | |
| D | GLN102 | |
| D | ASP168 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | ARG109 | |
| A | THR246 | |
| B | ARG109 | |
| B | THR246 | |
| C | ARG109 | |
| C | THR246 | |
| D | ARG109 | |
| D | THR246 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | ALA138 | |
| B | ALA138 | |
| C | ALA138 | |
| D | ALA138 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | ASN140 | |
| D | ASN140 | |
| D | ARG173 | |
| D | HIS188 | |
| A | ARG173 | |
| A | HIS188 | |
| B | ASN140 | |
| B | ARG173 | |
| B | HIS188 | |
| C | ASN140 | |
| C | ARG173 | |
| C | HIS188 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
| Chain | Residue | Details |
| A | SER163 | |
| B | SER163 | |
| C | SER163 | |
| D | SER163 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | TYR237 | |
| B | TYR237 | |
| C | TYR237 | |
| D | TYR237 |
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 |
