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 (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 |
A | 0051287 | molecular_function | NAD binding |
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 |
B | 0051287 | molecular_function | NAD binding |
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 |
C | 0051287 | molecular_function | NAD binding |
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 |
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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
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 | 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 |