7OCQ

NADH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii

Summary for 7OCQ

• Entry DOI: 10.2210/pdb7ocq/pdb
• Descriptor: HAD hydrolase, family IA, variant 3, [[(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, MAGNESIUM ION, ... (10 entities in total)
• Functional Keywords: mannitol, dehydrogenase, phosphatase, nadph, fructose-6-phosphate, oxidoreductase, had hydrolase family ia variant 3
• Biological source: Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81)
• Total number of polymer chains: 2
• Total formula weight: 169680.19

Authors

Tam, H.K.,Mueller, V.,Pos, K.M. (deposition date: 2021-04-28, release date: 2022-04-20, Last modification date: 2024-01-31)

• Primary citation: Tam, H.K.,Konig, P.,Himpich, S.,Ngu, N.D.,Abele, R.,Muller, V.,Pos, K.M.; Unidirectional mannitol synthesis of Acinetobacter baumannii MtlD is facilitated by the helix-loop-helix-mediated dimer formation.; Proc.Natl.Acad.Sci.USA, 119:e2107994119-e2107994119, 2022; PubMed: 35363566; DOI: 10.1073/pnas.2107994119

Experimental method

X-RAY DIFFRACTION (2.9 Å)