4ND1
Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with cofactor (b-nicotinamide adenine dinucleotide) and inhibitor (oxamic acid)
Replaces: 2FNZFunctional 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY30 |
| A | ILE138 |
| A | ASN140 |
| A | MET163 |
| A | LEU167 |
| A | HIS195 |
| A | GLU223 |
| A | ALA246 |
| A | OXM402 |
| A | HOH604 |
| A | HOH607 |
| A | GLN31 |
| A | HOH615 |
| A | HOH619 |
| A | HOH640 |
| A | HOH652 |
| A | HOH659 |
| A | ILE32 |
| A | ASP53 |
| A | ILE54 |
| A | THR97 |
| A | ALA98 |
| A | SER99 |
| A | ILE119 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OXM A 402 |
| Chain | Residue |
| A | ARG109 |
| A | ASN140 |
| A | LEU167 |
| A | ARG171 |
| A | HIS195 |
| A | TRP236 |
| A | ALA246 |
| A | NAD401 |
| A | HOH602 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | PRO201 |
| A | THR203 |
| A | GLU311 |
| A | LEU314 |
| A | HOH693 |
| A | HOH694 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | PRO141 |
| A | LEU142 |
| A | ASP143 |
| A | VAL144 |
| A | HIS195 |
| A | GLU321 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | PRO333 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | GLY30 |
| B | GLN31 |
| B | ILE32 |
| B | ASP53 |
| B | ILE54 |
| B | THR97 |
| B | ALA98 |
| B | SER99 |
| B | ILE119 |
| B | ILE138 |
| B | ASN140 |
| B | MET163 |
| B | LEU167 |
| B | HIS195 |
| B | ALA246 |
| B | PRO250 |
| B | OXM402 |
| B | HOH531 |
| B | HOH532 |
| B | HOH535 |
| B | HOH536 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM B 402 |
| Chain | Residue |
| B | ARG109 |
| B | ASN140 |
| B | LEU167 |
| B | ARG171 |
| B | HIS195 |
| B | TRP236 |
| B | NAD401 |
| B | HOH545 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | VAL200 |
| B | PRO201 |
| B | THR203 |
| B | GLU311 |
| B | LEU314 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 29 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IAVIGsGQIGgniayivgkdnladVVlFD |
| Chain | Residue | Details |
| A | ILE24-ASP53 |
| site_id | PS00659 |
| Number of Residues | 10 |
| Details | GLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LLGESINEVN |
| Chain | Residue | Details |
| A | LEU314-ASN323 |
