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 (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| 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 (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| 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 | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 66 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"838465","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07195","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07195","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07195","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
