1t2f Summary

pdbe.org/1t2f
spacer

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

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