1mbb Summary



The structure was published by Lees, W.J., Benson, T.E., Hogle, J.M., and Walsh, C.T., in 1996 in a paper entitled "(E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB)." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1995.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE. This molecule has the UniProt identifier P08373 (MURB_ECOLI)search. The sample contained 342 residues which is 100% of the natural sequence. Out of 342 residues 340 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE P08373 (1-342) (MURB_ECOLI)search Escherichia coli K-12search 99% 342 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P08373) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domainsearch, Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domainsearch Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 1search, Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2search, Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3search PF01565: FAD binding domainsearch, PF02873: UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P08373) oxidation-reduction processsearch peptidoglycan biosynthetic processsearch cell wall organizationsearch cell cyclesearch regulation of cell shapesearch cell divisionsearch flavin adenine dinucleotide bindingsearch catalytic activitysearch UDP-N-acetylmuramate dehydrogenase activitysearch oxidoreductase activitysearch oxidoreductase activity, acting on CH-OH group of donorssearch cytoplasmsearch

Chain InterPro annotation
A UDP-N-acetylenolpyruvoylglucosamine reductasesearch FAD linked oxidase, N-terminalsearch UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminalsearch FAD-binding, type 2search FAD-binding, type 2, subdomain 1search CO dehydrogenase flavoprotein-like, FAD-binding, subdomain 2search