1LLC
STRUCTURE DETERMINATION OF THE ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS CASEI AT 3.0 ANGSTROMS RESOLUTION
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 |
Functional Information from PDB Data
| site_id | AFP |
| Number of Residues | 7 |
| Details | RESIDUES CLOSE TO THE MOLECULAR P AXIS THAT BIND THE ALLOSTERIC ACTIVATOR |
| Chain | Residue |
| A | THR169 |
| A | ARG173 |
| A | HIS188 |
| A | TYR190 |
| A | ARG256 |
| A | VAL268 |
| A | LEU269 |
| site_id | SO4 |
| Number of Residues | 3 |
| Details | RESIDUES BINDING THE SULFATE |
| Chain | Residue |
| A | THR246 |
| A | ARG171 |
| A | HIS195 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. MGEHGDT |
| Chain | Residue | Details |
| A | MET192-THR198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.6, ECO:0000305|Ref.8, ECO:0007744|PDB:1LLC, ECO:0007744|PDB:6J9T, ECO:0007744|PDB:6J9U |
| Chain | Residue | Details |
| A | GLY196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | GLY33 | |
| A | ALA189 | |
| A | ILE54 | |
| A | THR59 | |
| A | SER86 | |
| A | ALA100 | |
| A | GLN103 | |
| A | ILE123 | |
| A | ALA139 | |
| A | GLY164 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.8, ECO:0007744|PDB:6J9U |
| Chain | Residue | Details |
| A | LEU110 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.8, ECO:0007744|PDB:6J9U |
| Chain | Residue | Details |
| A | PRO141 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.8, ECO:0007744|PDB:6J9S, ECO:0007744|PDB:6J9T, ECO:0007744|PDB:6J9U |
| Chain | Residue | Details |
| A | THR169 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.8, ECO:0007744|PDB:6J9T, ECO:0007744|PDB:6J9U |
| Chain | Residue | Details |
| A | GLN174 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:6J9T |
| Chain | Residue | Details |
| A | SER186 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.8, ECO:0007744|PDB:6J9S, ECO:0007744|PDB:6J9U |
| Chain | Residue | Details |
| A | PHE247 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
| Chain | Residue | Details |
| A | GLU238 |
