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 | 0008152 | biological_process | metabolic 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 | 0008152 | biological_process | metabolic 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 |
