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 activity |
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 | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004459 | molecular_function | L-lactate dehydrogenase activity |
C | 0006089 | biological_process | lactate metabolic process |
C | 0006090 | biological_process | pyruvate 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 activity |
D | 0006089 | biological_process | lactate metabolic process |
D | 0006090 | biological_process | pyruvate 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 |