1LDB
STRUCTURE DETERMINATION AND REFINEMENT OF BACILLUS STEAROTHERMOPHILUS LACTATE DEHYDROGENASE
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 |
| A | 0051287 | molecular_function | NAD binding |
| 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 |
| B | 0051287 | molecular_function | NAD binding |
| 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 |
| C | 0051287 | molecular_function | NAD binding |
| 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 |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | ARG169 |
| A | HIS193 |
| A | ALA237 |
| A | THR247 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | HIS186 |
| A | TYR188 |
| D | ASN184 |
| D | HIS186 |
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 | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN |
| Chain | Residue | Details |
| A | HIS193 | |
| B | HIS193 | |
| C | HIS193 | |
| D | HIS193 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB |
| Chain | Residue | Details |
| A | PHE30 | |
| D | PHE30 | |
| D | ASP52 | |
| D | ALA136 | |
| A | ASP52 | |
| A | ALA136 | |
| B | PHE30 | |
| B | ASP52 | |
| B | ALA136 | |
| C | PHE30 | |
| C | ASP52 | |
| C | ALA136 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | LYS57 | |
| B | GLN100 | |
| B | SER119 | |
| B | ASN138 | |
| C | LYS57 | |
| C | TYR83 | |
| C | GLY97 | |
| C | GLN100 | |
| C | SER119 | |
| C | ASN138 | |
| D | LYS57 | |
| A | TYR83 | |
| D | TYR83 | |
| D | GLY97 | |
| D | GLN100 | |
| D | SER119 | |
| D | ASN138 | |
| A | GLY97 | |
| A | GLN100 | |
| A | SER119 | |
| A | ASN138 | |
| B | LYS57 | |
| B | TYR83 | |
| B | GLY97 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN |
| Chain | Residue | Details |
| A | ARG106 | |
| D | ARG106 | |
| D | ASP166 | |
| D | THR247 | |
| A | ASP166 | |
| A | THR247 | |
| B | ARG106 | |
| B | ASP166 | |
| B | THR247 | |
| C | ARG106 | |
| C | ASP166 | |
| C | THR247 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB |
| Chain | Residue | Details |
| A | SER161 | |
| A | GLN183 | |
| B | SER161 | |
| B | GLN183 | |
| C | SER161 | |
| C | GLN183 | |
| D | SER161 | |
| D | GLN183 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:2LDB |
| Chain | Residue | Details |
| A | ARG171 | |
| B | ARG171 | |
| C | ARG171 | |
| D | ARG171 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | TYR238 | |
| B | TYR238 | |
| C | TYR238 | |
| D | TYR238 |
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 | 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 | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS193 | |
| A | ASP166 | |
| A | ARG169 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS193 | |
| B | ASP166 | |
| B | ARG169 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS193 | |
| C | ASP166 | |
| C | ARG169 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS193 | |
| D | ASP166 | |
| D | ARG169 |
