1SOW
T. gondii bradyzoite-specific LDH (LDH2) in complex with NAD and oxalate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OXL A 402 |
| Chain | Residue |
| A | TRP107 |
| A | ARG109 |
| A | ASN140 |
| A | ARG171 |
| A | HIS195 |
| A | GLY236 |
| A | NAD401 |
| A | HOH419 |
| A | HOH437 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OXL B 502 |
| Chain | Residue |
| B | TRP107 |
| B | ARG109 |
| B | ASN140 |
| B | ARG171 |
| B | HIS195 |
| B | GLY236 |
| B | ALA246 |
| B | NAD501 |
| B | HOH505 |
| B | HOH525 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY29 |
| A | MET30 |
| A | ILE31 |
| A | ASP53 |
| A | VAL54 |
| A | VAL55 |
| A | MET58 |
| A | THR97 |
| A | ALA98 |
| A | GLY99 |
| A | LEU100 |
| A | THR101 |
| A | ILE119 |
| A | GLU122 |
| A | VAL138 |
| A | THR139 |
| A | ASN140 |
| A | MET163 |
| A | LEU167 |
| A | HIS195 |
| A | ALA246 |
| A | OXL402 |
| A | HOH411 |
| A | HOH416 |
| A | HOH419 |
| A | HOH425 |
| A | HOH453 |
| A | HOH466 |
| A | HOH511 |
| A | HOH512 |
| A | HOH532 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | GLY29 |
| B | MET30 |
| B | ILE31 |
| B | PHE52 |
| B | ASP53 |
| B | VAL54 |
| B | VAL55 |
| B | MET58 |
| B | THR97 |
| B | ALA98 |
| B | GLY99 |
| B | LEU100 |
| B | THR101 |
| B | GLU122 |
| B | VAL138 |
| B | THR139 |
| B | ASN140 |
| B | MET163 |
| B | LEU167 |
| B | HIS195 |
| B | ALA246 |
| B | OXL502 |
| B | HOH504 |
| B | HOH505 |
| B | HOH509 |
| B | HOH519 |
| B | HOH615 |
| B | HOH617 |
| B | HOH631 |
| B | HOH632 |
| B | HOH653 |
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 | HIS195 | |
| B | HIS195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP53 | |
| A | ARG109 | |
| A | ASN140 | |
| A | ARG171 | |
| B | ASP53 | |
| B | ARG109 | |
| B | ASN140 | |
| B | ARG171 |
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 |
