1j49 Summary

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INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS

The structure was published by Razeto, A., Kochhar, S., Hottinger, H., Dauter, M., Wilson, K.S., and Lamzin, V.S., in 2002 in a paper entitled "Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2001.

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

This PDB entry contains multiple copies of the structure of D-LACTATE DEHYDROGENASE.

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 homodimers.

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 D-LACTATE DEHYDROGENASE P26297 (1-333) (LDHD_LACDA)search Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842search 100% 333 99%
B D-LACTATE DEHYDROGENASE P26297 (1-333) (LDHD_LACDA)search Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842search 100% 333 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P26297 (1 - 333) D-LACTATE DEHYDROGENASE Lactobacillus delbrueckii subsp. bulgaricus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P26297) Formate/glycerate dehydrogenases, NAD-domainsearch, Formate/glycerate dehydrogenases, substrate-binding domainsearch NAD(P)-binding Rossmann-like Domainsearch PF00389: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P26297) NAD bindingsearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch oxidoreductase activitysearch D-lactate dehydrogenase activitysearch metabolic processsearch oxidation-reduction processsearch

Chain InterPro annotation
A, B D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domainsearch D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domainsearch NAD(P)-binding domainsearch D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1search D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved sitesearch