1LTH
T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| R | 0003824 | molecular_function | catalytic activity |
| R | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| R | 0005737 | cellular_component | cytoplasm |
| R | 0006089 | biological_process | lactate metabolic process |
| R | 0006090 | biological_process | pyruvate metabolic process |
| R | 0006096 | biological_process | glycolytic process |
| R | 0008152 | biological_process | metabolic process |
| R | 0016491 | molecular_function | oxidoreductase activity |
| R | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| R | 0019752 | biological_process | carboxylic acid metabolic process |
| T | 0003824 | molecular_function | catalytic activity |
| T | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| T | 0005737 | cellular_component | cytoplasm |
| T | 0006089 | biological_process | lactate metabolic process |
| T | 0006090 | biological_process | pyruvate metabolic process |
| T | 0006096 | biological_process | glycolytic process |
| T | 0008152 | biological_process | metabolic process |
| T | 0016491 | molecular_function | oxidoreductase activity |
| T | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| T | 0019752 | biological_process | carboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | RFB |
| Number of Residues | 5 |
| Details | FBP BINDING SITE IN THE R CHAIN |
| Chain | Residue |
| R | ARG158 |
| R | LYS170 |
| R | ASN171 |
| R | HIS173 |
| R | TYR175 |
| site_id | RND |
| Number of Residues | 18 |
| Details | NADH BINDING SITE IN THE R CHAIN |
| Chain | Residue |
| R | ILE13 |
| R | GLY16 |
| R | ALA17 |
| R | VAL18 |
| R | ASP39 |
| R | ILE40 |
| R | THR82 |
| R | ALA83 |
| R | GLY84 |
| R | PRO85 |
| R | ARG86 |
| R | ILE103 |
| R | ILE107 |
| R | ILE123 |
| R | THR124 |
| R | ASN125 |
| R | HIS180 |
| R | ILE240 |
| site_id | ROX |
| Number of Residues | 8 |
| Details | OXAMATE BINDING SITE IN THE R CHAIN |
| Chain | Residue |
| R | GLN87 |
| R | ARG93 |
| R | ASN125 |
| R | LEU152 |
| R | ARG156 |
| R | HIS180 |
| R | ALA226 |
| R | THR236 |
| site_id | TFB |
| Number of Residues | 5 |
| Details | FBP BINDING SITE IN THE T CHAIN |
| Chain | Residue |
| T | ARG158 |
| T | LYS170 |
| T | ASN171 |
| T | HIS173 |
| T | TYR175 |
| site_id | TND |
| Number of Residues | 20 |
| Details | NADH BINDING SITE IN THE T CHAIN |
| Chain | Residue |
| T | ILE13 |
| T | GLY84 |
| T | ARG86 |
| T | ILE103 |
| T | ILE107 |
| T | ILE123 |
| T | THR124 |
| T | ASN125 |
| T | HIS180 |
| T | ILE230 |
| T | ASN237 |
| T | GLY16 |
| T | ILE240 |
| T | ALA17 |
| T | VAL18 |
| T | ASP39 |
| T | ILE40 |
| T | ARG44 |
| T | THR82 |
| T | ALA83 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. AGEHGDS |
| Chain | Residue | Details |
| T | 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 |
| T | GLY181 | |
| R | GLY181 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| T | GLY19 | |
| R | ALA174 | |
| T | LYS88 | |
| T | LEU94 | |
| T | GLY149 | |
| T | ALA174 | |
| R | GLY19 | |
| R | LYS88 | |
| R | LEU94 | |
| R | 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 |
| T | ILE40 | |
| T | THR124 | |
| R | ILE40 | |
| R | THR124 | |
| T | VAL18 | |
| R | 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 |
| T | VAL45 | |
| R | 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 |
| T | PRO126 | |
| T | SER154 | |
| T | ASN237 | |
| R | PRO126 | |
| R | SER154 | |
| R | 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 |
| T | PHE159 | |
| R | PHE159 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| T | LYS228 | |
| R | LYS228 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7656036, ECO:0007744|PDB:1LTH |
| Chain | Residue | Details |
| T | ASN171 | |
| R | ASN171 |
