3PQE
Crystal structure of L-lactate dehydrogenase from Bacillus subtilis with H171C mutation
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 | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate 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 activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate 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 activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006090 | biological_process | pyruvate 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 activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006090 | biological_process | pyruvate 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 |
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 | ILE175-THR181 |
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|Ref.7, ECO:0007744|PDB:3PQD |
| Chain | Residue | Details |
| A | HIS178 | |
| B | HIS178 | |
| C | HIS178 | |
| D | HIS178 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD, ECO:0007744|PDB:3PQF |
| Chain | Residue | Details |
| C | PHE15 | |
| D | PHE15 | |
| A | PHE15 | |
| B | PHE15 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.7, ECO:0007744|PDB:3PQF |
| Chain | Residue | Details |
| C | ASP37 | |
| C | GLY82 | |
| D | ASP37 | |
| D | GLY82 | |
| A | ASP37 | |
| A | GLY82 | |
| B | ASP37 | |
| B | GLY82 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | ASN123 | |
| A | SER146 | |
| A | ASP151 | |
| A | THR232 | |
| B | LYS42 | |
| B | TYR68 | |
| B | GLN85 | |
| B | ARG91 | |
| B | ASN123 | |
| B | SER146 | |
| B | ASP151 | |
| B | THR232 | |
| C | LYS42 | |
| C | TYR68 | |
| C | GLN85 | |
| C | ARG91 | |
| C | ASN123 | |
| C | SER146 | |
| C | ASP151 | |
| C | THR232 | |
| D | LYS42 | |
| D | TYR68 | |
| D | GLN85 | |
| D | ARG91 | |
| D | ASN123 | |
| D | SER146 | |
| D | ASP151 | |
| D | THR232 | |
| A | LYS42 | |
| A | TYR68 | |
| A | GLN85 | |
| A | ARG91 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.7, ECO:0007744|PDB:3PQD |
| Chain | Residue | Details |
| C | ALA121 | |
| D | ALA121 | |
| A | ALA121 | |
| B | ALA121 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD |
| Chain | Residue | Details |
| C | ARG156 | |
| D | ARG156 | |
| A | ARG156 | |
| B | ARG156 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD |
| Chain | Residue | Details |
| A | GLN168 | |
| B | GLN168 | |
| C | GLN168 | |
| D | GLN168 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17218307 |
| Chain | Residue | Details |
| A | TYR223 | |
| B | TYR223 | |
| C | TYR223 | |
| D | TYR223 |
