DTDP-glucose 4,6-dehydratase

spinqualitylabelsall models RmlB dimer complex with NAD, TDP-D-glucose and sulfate (PDB code 1ker) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function dTDP-glucose 4,6-dehydratase (RmlB) catalyzes the reversible conversion of dTDP-glucose to dTDP-4-dehydro-6-deoxy-D-glucose. RmlB is the second of four enzymes involved in the dTDP-L-rhamnose pathway. RmlB is involved in the pathway LSP O-antigen biosynthesis which is part of the bacterial outer membrane biogenesis. Structural highlights The RmlB structure is divided into 2 domains. The N-terminal NAD-binding domain which contains the Rossmann fold and the C-terminal sugar nucleotide binding domain. NAD binding site. TDB-glucose binding site. Whole active site.

3D structures of RmlB

Updated on 07-February-2023

1kep, 1oc2 – SsRmlB + NAD + TDP-xylose – Streptococcus suis
1ker – SsRmlB + NAD + TDP-glucose
1ket – SsRmlB + NAD + TDP
1keu – StRmlB + NAD + TDP-glucose – Salmonella typhimurium
1kew – StRmlB + NAD + TDP
1g1a – StRmlB + NAD
1bxk – EcRmlB + NAD – Escherichia coli
1r66, 1r6d – RmlB + NAD + TDP derivative – Streptococcus venezuelae
6bi4 – RmlB + NAD + TDP-sucrose – Bacillus anthracis
5u4q – RmlB + NAD – Klebsiella pneumoniae
6bwl – RmlB + NAD + UDP – Bacillus thuringiensis
8du1 – RmlB + NAD – Elizabethkingia anophelis

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