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Structure paper

TitleDifferent ways to transport ammonia in human and Mycobacterium tuberculosis NAD+synthetases.
Journal, issue, pagesNat Commun, Vol. 11, Page 16-16, Year 2020
Publish dateMar 28, 2019 (structure data deposition date)
AuthorsChuenchor, W. / Doukov, T.I. / Chang, K.T. / Resto, M. / Yun, C.S. / Gerratana, B.
External linksNat Commun / PubMed:31911602
MethodsX-ray diffraction
Resolution2.84 - 3.14 Å
Structure data

PDB-6ofb:
Crystal structure of human glutamine-dependent NAD+ synthetase complexed with NaAD+, AMP, pyrophosphate, and Mg2+
Method: X-RAY DIFFRACTION / Resolution: 2.84 Å

PDB-6ofc:
Crystal structure of M. tuberculosis glutamine-dependent NAD+ synthetase complexed with Sulfonamide derivative 1, pyrophosphate, and glutamine
Method: X-RAY DIFFRACTION / Resolution: 3.14 Å

Chemicals

ChemComp-DND:
NICOTINIC ACID ADENINE DINUCLEOTIDE

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-POP:
PYROPHOSPHATE 2-

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SFH:
5'-O-[(pyridine-3-carbonyl)sulfamoyl]adenosine

ChemComp-GLN:
GLUTAMINE

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
  • mycobacterium tuberculosis cdc1551 (bacteria)
KeywordsLIGASE / GLUTAMINE-AMIDO TRANSFERASE / GAT / NAD+ SYNTHETASE / GLUTAMINE-DEPENDENT NAD+ SYNTHETASE / NAD SYNTHETASE 1 / GLUTAMINASE / AMMONIA TUNNELING / ENZYME / ATP-BINDING / NUCLEOTIDE-BINDING / INHIBITOR COMPLEX / TUBERCULOSIS

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