Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2FN7

Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (lactic acid) and cofactor (b-nicotinamide adenine dinucleotide)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase activity
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues29
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IAVIGsGQIGgniayivgkdnladVVlFD
ChainResidueDetails
AILE23-ASP53

site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LLGESINEVN
ChainResidueDetails
ALEU314-ASN323

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS195
AASP168

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS195
BASP168

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS195
AARG171
AASP168

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS195
BARG171
BASP168

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon