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 |