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

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