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TitleMutations of endo-beta-N-acetylglucosaminidase H active site residues Asp130 and Glu132: activities and conformations.
Journal, issue, pagesProtein Sci., Vol. 8, Page 2338-2346, Year 1999
Publish dateJul 27, 1999 (structure data deposition date)
AuthorsRao, V. / Cui, T. / Guan, C. / Van Roey, P.
External linksPubMed:10595536
MethodsX-ray diffraction
Resolution2 - 2.1 Å
Structure data

PDB-1c3f:
Endo-Beta-N-Acetylglucosaminidase H, D130N Mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1c8x:
Endo-Beta-N-Acetylglucosaminidase H, D130E Mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1c8y:
Endo-Beta-N-Acetylglucosaminidase H, D130A Mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1c90:
Endo-Beta-N-Acetylglucosaminidase H, E132Q Mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1c91:
Endo-Beta-N-Acetylglucosaminidase H, E132D
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1c92:
Endo-Beta-N-Acetylglucosaminidase H, E132A Mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1c93:
Endo-Beta-N-Acetylglucosaminidase H, D130N/E132Q Double Mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ZN:
Unknown entry

Source
  • streptomyces plicatus (bacteria)
KeywordsHYDROLASE / (BETA-ALPHA)8-BARREL / (ALPHA/BETA)8-BARREL / (BETA/ALPHA)8-BARREL / (BETA/ALPHA)8 BARREL

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