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Structure paper

TitleStructural basis of catalysis and substrate recognition by the NAD(H)-dependent alpha-d-glucuronidase from the glycoside hydrolase family 4.
Journal, issue, pagesBiochem. J., Vol. 478, Page 943-959, Year 2021
Publish dateAug 18, 2020 (structure data deposition date)
AuthorsMohapatra, S.B. / Manoj, N.
External linksBiochem. J. / PubMed:33565573
MethodsX-ray diffraction
Resolution1.85 - 2.15 Å
Structure data

PDB-7ctd:
Crystal structure of apo form of alpha-glucuronidase (TM0752) from Thermotoga maritima
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-7ctl:
Crystal structure of NADH bound holo form of alpha-glucuronidase (TM0752) from Thermotoga maritima at 1.97 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-7ctm:
Crystal structure of Thermotoga maritima alpha-glucuronidase (TM0752) in complex with NADH and D-glucuronic acid
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-BDP:
beta-D-glucopyranuronic acid

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

Source
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
KeywordsHYDROLASE / Glycosyl hydrolase family 4 / NAD(P)-binding Rossmann-fold domain / LDH C-terminal domain-like / hydrolase activity / alpha-glucuronidase

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