NADH bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate DEHYDROGENASE/PHOSPHATASE mtld from acinetobacter baumannii

Structure

x-ray diffraction · 2 distinct chains.

Ligands and binding sites

• V8H · [[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonyl-4~{H}-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-3,4,5-tris(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate · ligand · chains A
• NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains B
• MG · Magnesium ion · metal · 2 copies · chains A, B
• CL · Chloride ion · ion · 7 copies · chains A, B
• SO4 · Sulfate ion · ion · 3 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 2 copies · chains A
• GOL · Glycerol · additive · 2 copies · chains A, B
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

• 7OCQ · NADH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt D0C7J2
• Elsewhere: RCSB PDB 7OCQ · PDBe 7OCQ · UniProt D0C7J2