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TitleStructure and mechanism of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis
Journal, issue, pagesStructure, Vol. 11, Page 1015-1023, Year 2003
Publish dateAug 28, 2002 (structure data deposition date)
AuthorsKang, L.-W. / Gabelli, S.B. / Cunningham, J.E. / O'Handley, S.F. / Amzel, L.M.
External linksStructure / PubMed:12906832
MethodsX-ray diffraction
Resolution2 - 2.3 Å
Structure data

PDB-1mk1:
Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1mp2:
Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1mqe:
Structure of the MT-ADPRase in complex with gadolidium and ADP-ribose, a Nudix enzyme
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1mqw:
Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1mr2:
Structure of the MT-ADPRase in complex with 1 Mn2+ ion and AMP-CP (a inhibitor), a nudix enzyme
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-APR:
ADENOSINE-5-DIPHOSPHORIBOSE

ChemComp-HOH:
WATER

ChemComp-GD3:
GADOLINIUM ION

ChemComp-MN:
Unknown entry

ChemComp-ADV:
ALPHA-BETA METHYLENE ADP-RIBOSE

ChemComp-A12:
PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / Nudix hydrolase / ADPR pyrophosphatase / ADPRase / Adenosine diphospho-ribose / Mycobacterium Tuberculosis / Rv1700 / ADPR

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