1PZG
T.gondii LDH1 complexed with APAD and sulfate at 1.6 Angstroms
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 | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | TRP107 |
| A | ARG109 |
| A | ASN140 |
| A | ARG171 |
| A | HIS195 |
| A | GLY236 |
| A | ALA246 |
| A | A3D601 |
| A | HOH642 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 604 |
| Chain | Residue |
| B | TRP107 |
| B | ARG109 |
| B | ASN140 |
| B | LEU167 |
| B | ARG171 |
| B | HIS195 |
| B | GLY236 |
| B | ALA246 |
| B | A3D603 |
| B | HOH618 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 606 |
| Chain | Residue |
| C | TRP107 |
| C | ARG109 |
| C | ARG171 |
| C | HIS195 |
| C | GLY236 |
| C | A3D605 |
| C | HOH639 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 D 608 |
| Chain | Residue |
| D | TRP107 |
| D | ARG109 |
| D | LEU167 |
| D | ARG171 |
| D | HIS195 |
| D | GLY236 |
| D | ALA246 |
| D | A3D607 |
| D | HOH635 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE A3D A 601 |
| Chain | Residue |
| A | GLY29 |
| A | MET30 |
| A | ILE31 |
| A | TYR52 |
| A | ASP53 |
| A | VAL54 |
| A | VAL55 |
| A | MET58 |
| A | THR97 |
| A | ALA98 |
| A | GLY99 |
| A | LEU100 |
| A | THR101 |
| A | ILE119 |
| A | VAL138 |
| A | THR139 |
| A | ASN140 |
| A | LEU142 |
| A | MET163 |
| A | LEU167 |
| A | HIS195 |
| A | ALA246 |
| A | SO4602 |
| A | HOH605 |
| A | HOH610 |
| A | HOH659 |
| A | HOH678 |
| A | HOH694 |
| A | HOH710 |
| A | HOH760 |
| site_id | AC6 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE A3D B 603 |
| Chain | Residue |
| B | GLY29 |
| B | MET30 |
| B | ILE31 |
| B | ASP53 |
| B | VAL54 |
| B | VAL55 |
| B | MET58 |
| B | THR97 |
| B | ALA98 |
| B | GLY99 |
| B | LEU100 |
| B | THR101 |
| B | ILE119 |
| B | VAL138 |
| B | THR139 |
| B | ASN140 |
| B | LEU142 |
| B | MET163 |
| B | LEU167 |
| B | HIS195 |
| B | ALA246 |
| B | PRO250 |
| B | SO4604 |
| B | HOH615 |
| B | HOH619 |
| B | HOH651 |
| B | HOH686 |
| B | HOH716 |
| B | HOH744 |
| B | HOH748 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE A3D C 605 |
| Chain | Residue |
| C | ASP53 |
| C | VAL54 |
| C | VAL55 |
| C | MET58 |
| C | THR97 |
| C | ALA98 |
| C | GLY99 |
| C | LEU100 |
| C | THR101 |
| C | ILE119 |
| C | VAL138 |
| C | ASN140 |
| C | LEU142 |
| C | MET163 |
| C | LEU167 |
| C | HIS195 |
| C | ALA246 |
| C | SO4606 |
| C | HOH613 |
| C | HOH622 |
| C | HOH694 |
| C | HOH721 |
| C | HOH723 |
| C | GLY29 |
| C | MET30 |
| C | ILE31 |
| C | TYR52 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE A3D D 607 |
| Chain | Residue |
| D | GLY29 |
| D | MET30 |
| D | ILE31 |
| D | ASP53 |
| D | VAL54 |
| D | VAL55 |
| D | MET58 |
| D | THR97 |
| D | ALA98 |
| D | GLY99 |
| D | LEU100 |
| D | THR101 |
| D | ILE119 |
| D | VAL138 |
| D | THR139 |
| D | ASN140 |
| D | LEU142 |
| D | MET163 |
| D | LEU167 |
| D | HIS195 |
| D | ALA246 |
| D | SO4608 |
| D | HOH612 |
| D | HOH628 |
| D | HOH645 |
| D | HOH716 |
| D | HOH727 |
| D | HOH729 |
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 |
