1t2f Summary


Human B lactate dehydrogenase complexed with NAD+ and 4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid

The structure was published by Cameron, A., Read, J., Tranter, R., et al., Gabarro, R., Mallo, A., and De Las Heras, F.G., in 2004 in a paper entitled "Identification and Activity of a Series of Azole-based Compounds with Lactate Dehydrogenase-directed Anti-malarial Activity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of L-lactate dehydrogenase B chain.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A L-lactate dehydrogenase B chain P07195 (2-332) (LDHB_HUMAN)search Homo sapienssearch 99% 333 99%
B L-lactate dehydrogenase B chain P07195 (2-332) (LDHB_HUMAN)search Homo sapienssearch 99% 333 99%
C L-lactate dehydrogenase B chain P07195 (2-332) (LDHB_HUMAN)search Homo sapienssearch 99% 333 99%
D L-lactate dehydrogenase B chain P07195 (2-332) (LDHB_HUMAN)search Homo sapienssearch 99% 333 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07195 (2 - 332) L-lactate dehydrogenase B chain Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P07195) LDH N-terminal domain-likesearch, Lactate & malate dehydrogenases, C-terminal domainsearch NAD(P)-binding Rossmann-like Domainsearch, L-2-Hydroxyisocaproate Dehydrogenase, subunit A, domain 2search PF00056: lactate/malate dehydrogenase, NAD binding domainsearch, PF02866: lactate/malate dehydrogenase, alpha/beta C-terminal domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B, C, D (P07195) NAD bindingsearch L-lactate dehydrogenase activitysearch protein bindingsearch kinase bindingsearch identical protein bindingsearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch oxidoreductase activitysearch lactate dehydrogenase activitysearch catalytic activitysearch extracellular vesicular exosomesearch cytosolsearch mitochondrionsearch cytoplasmsearch membranesearch cellular metabolic processsearch small molecule metabolic processsearch oxidation-reduction processsearch carbohydrate metabolic processsearch cellular carbohydrate metabolic processsearch pyruvate metabolic processsearch NAD metabolic processsearch lactate metabolic processsearch

Chain InterPro annotation
A, B, C, D Lactate/malate dehydrogenase, N-terminalsearch L-lactate/malate dehydrogenasesearch L-lactate dehydrogenasesearch Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminalsearch NAD(P)-binding domainsearch L-lactate dehydrogenase, active sitesearch Lactate/malate dehydrogenase, C-terminalsearch