1LLD
MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-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 |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD A 320 |
Chain | Residue |
A | GLY16 |
A | ALA17 |
A | VAL18 |
A | ASP39 |
A | ILE40 |
A | ARG44 |
A | THR82 |
A | ALA83 |
A | GLY84 |
A | ILE107 |
A | ASN125 |
A | HIS180 |
A | ASN237 |
A | ILE240 |
A | HOH324 |
A | HOH340 |
A | HOH356 |
A | HOH360 |
A | HOH386 |
A | HOH396 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAD B 320 |
Chain | Residue |
B | GLY16 |
B | ALA17 |
B | VAL18 |
B | ASP39 |
B | ILE40 |
B | THR82 |
B | ALA83 |
B | GLY84 |
B | ARG86 |
B | ILE107 |
B | ILE123 |
B | THR124 |
B | ASN125 |
B | HIS180 |
B | ASN237 |
B | ILE240 |
B | HOH338 |
B | HOH339 |
B | HOH347 |
site_id | AND |
Number of Residues | 15 |
Details | RESIDUES FORMING THE NADH BINDING SITES OF A SUBUNIT |
Chain | Residue |
A | ILE13 |
A | ILE107 |
A | ILE123 |
A | ASN125 |
A | ILE229 |
A | ILE230 |
A | ILE240 |
A | GLY14 |
A | ALA17 |
A | VAL18 |
A | ASP39 |
A | ILE40 |
A | ARG44 |
A | ALA83 |
A | ILE103 |
site_id | BND |
Number of Residues | 15 |
Details | RESIDUES FORMING THE NADH BINDING SITES OF B SUBUNIT |
Chain | Residue |
B | ILE13 |
B | GLY14 |
B | ALA17 |
B | VAL18 |
B | ASP39 |
B | ILE40 |
B | ALA83 |
B | ARG86 |
A | ILE103 |
A | ILE107 |
A | ILE123 |
A | ASN125 |
A | ILE229 |
A | ILE230 |
A | ILE240 |
Functional Information from PROSITE/UniProt
site_id | PS00064 |
Number of Residues | 7 |
Details | L_LDH L-lactate dehydrogenase active site. AGEHGDS |
Chain | Residue | Details |
A | ALA177-SER183 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:7656036, ECO:0007744|PDB:1LTH |
Chain | Residue | Details |
A | GLY181 | |
B | GLY181 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | GLY19 | |
B | ALA174 | |
A | LYS88 | |
A | LEU94 | |
A | GLY149 | |
A | ALA174 | |
B | GLY19 | |
B | LYS88 | |
B | LEU94 | |
B | GLY149 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:7656036, ECO:0000269|PubMed:8450537, ECO:0007744|PDB:1LLD, ECO:0007744|PDB:1LTH |
Chain | Residue | Details |
A | ILE40 | |
A | THR124 | |
B | ILE40 | |
B | THR124 | |
A | VAL18 | |
B | VAL18 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7656036, ECO:0000269|PubMed:8450537, ECO:0007744|PDB:1LLD, ECO:0007744|PDB:1LTH |
Chain | Residue | Details |
A | VAL45 | |
B | VAL45 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:7656036, ECO:0007744|PDB:1LTH |
Chain | Residue | Details |
A | PRO126 | |
A | SER154 | |
A | ASN237 | |
B | PRO126 | |
B | SER154 | |
B | ASN237 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:7656036, ECO:0007744|PDB:1LTH |
Chain | Residue | Details |
A | PHE159 | |
B | PHE159 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | LYS228 | |
B | LYS228 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7656036, ECO:0007744|PDB:1LTH |
Chain | Residue | Details |
A | ASN171 | |
B | ASN171 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS180 | |
A | ASP153 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | HIS180 | |
B | ASP153 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | ARG156 | |
A | HIS180 | |
A | ASP153 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | ARG156 | |
B | HIS180 | |
B | ASP153 |