5LDH
STRUCTURE OF THE ACTIVE TERNARY COMPLEX OF PIG HEART LACTATE DEHYDROGENASE WITH S-LAC-NAD AT 2.7 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 | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate 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 | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate 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 | 19 |
| Details | BINDING SITE FOR RESIDUE LNC A 332 |
| Chain | Residue |
| A | GLY30 |
| A | GLN102 |
| A | ARG109 |
| A | VAL138 |
| A | SER163 |
| A | LEU167 |
| A | ARG171 |
| A | HIS195 |
| A | ALA236 |
| A | THR246 |
| A | ILE250 |
| A | GLN31 |
| A | VAL32 |
| A | ASP53 |
| A | LEU55 |
| A | LYS58 |
| A | THR97 |
| A | GLY99 |
| A | ARG101 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CIT A 333 |
| Chain | Residue |
| A | HIS188 |
| A | TRP190 |
| A | GLY209 |
| A | VAL209 |
| A | ILE268 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE LNC B 332 |
| Chain | Residue |
| B | GLY30 |
| B | GLN31 |
| B | VAL32 |
| B | ASP53 |
| B | LEU55 |
| B | LYS58 |
| B | THR97 |
| B | GLY99 |
| B | ARG101 |
| B | GLN102 |
| B | ARG109 |
| B | VAL138 |
| B | SER163 |
| B | LEU167 |
| B | ARG171 |
| B | HIS195 |
| B | ALA236 |
| B | THR246 |
| B | ILE250 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CIT B 333 |
| Chain | Residue |
| B | HIS188 |
| B | TRP190 |
| B | GLY209 |
| B | VAL209 |
| B | ILE268 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
| Chain | Residue | Details |
| A | LEU192-SER198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY196 | |
| B | GLY196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLN31 | |
| B | PRO141 | |
| B | PHE172 | |
| B | ASN247 | |
| A | GLN102 | |
| A | LEU110 | |
| A | PRO141 | |
| A | PHE172 | |
| A | ASN247 | |
| B | GLN31 | |
| B | GLN102 | |
| B | LEU110 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:838465 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07195 |
| Chain | Residue | Details |
| A | LEU7 | |
| A | LEU59 | |
| A | PHE122 | |
| A | ASP328 | |
| B | LEU7 | |
| B | LEU59 | |
| B | PHE122 | |
| B | ASP328 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07195 |
| Chain | Residue | Details |
| A | LEU45 | |
| B | LEU45 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07195 |
| Chain | Residue | Details |
| A | GLU238 | |
| B | GLU238 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ASP168 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ASP168 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ARG171 | |
| A | ASP168 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ARG171 | |
| B | ASP168 |
