2A92
Crystal structure of lactate dehydrogenase from Plasmodium vivax: complex with NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0006089 | biological_process | lactate 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| B | 0006089 | biological_process | lactate 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAI C 501 |
| Chain | Residue |
| C | GLY27 |
| C | THR97 |
| C | ALA98 |
| C | GLY99 |
| C | VAL138 |
| C | THR139 |
| C | ASN140 |
| C | LEU163 |
| C | LEU167 |
| C | HIS195 |
| C | HOH542 |
| C | GLY29 |
| C | HOH557 |
| C | HOH567 |
| C | HOH575 |
| C | HOH607 |
| C | MET30 |
| C | ILE31 |
| C | PHE52 |
| C | ASP53 |
| C | VAL54 |
| C | VAL55 |
| C | TYR85 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAI A 601 |
| Chain | Residue |
| A | GLY29 |
| A | MET30 |
| A | ILE31 |
| A | PHE52 |
| A | ASP53 |
| A | VAL54 |
| A | VAL55 |
| A | TYR85 |
| A | THR97 |
| A | ALA98 |
| A | GLY99 |
| A | ILE119 |
| A | VAL138 |
| A | ASN140 |
| A | VAL142 |
| A | LEU163 |
| A | LEU167 |
| A | HIS195 |
| A | HOH615 |
| A | HOH626 |
| A | HOH682 |
| A | HOH686 |
| A | HOH701 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAI B 701 |
| Chain | Residue |
| B | GLY29 |
| B | MET30 |
| B | ILE31 |
| B | PHE52 |
| B | ASP53 |
| B | VAL54 |
| B | VAL55 |
| B | TYR85 |
| B | THR97 |
| B | ALA98 |
| B | GLY99 |
| B | GLU122 |
| B | VAL138 |
| B | ASN140 |
| B | VAL142 |
| B | LEU163 |
| B | LEU167 |
| B | HIS195 |
| B | HOH718 |
| B | HOH779 |
| B | HOH799 |
| B | HOH813 |
| B | HOH830 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAI D 801 |
| Chain | Residue |
| D | GLY29 |
| D | MET30 |
| D | ILE31 |
| D | PHE52 |
| D | ASP53 |
| D | VAL55 |
| D | MET58 |
| D | TYR85 |
| D | THR97 |
| D | ALA98 |
| D | GLY99 |
| D | PHE100 |
| D | THR101 |
| D | VAL138 |
| D | ASN140 |
| D | LEU163 |
| D | LEU167 |
| D | HIS195 |
| D | HOH814 |
| D | HOH840 |
| D | HOH866 |
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 | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS195 | |
| C | ASP168 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS195 | |
| D | ASP168 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ARG171 | |
| A | ASP168 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ARG171 | |
| B | ASP168 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS195 | |
| C | ARG171 | |
| C | ASP168 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS195 | |
| D | ARG171 | |
| D | ASP168 |
