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TitleSearch of multiple hot spots on the surface of peptidyl-tRNA hydrolase: structural, binding and antibacterial studies.
Journal, issue, pagesBiochem. J., Vol. 475, Page 547-560, Year 2018
Publish dateAug 23, 2017 (structure data deposition date)
AuthorsKaushik, S. / Iqbal, N. / Singh, N. / Sikarwar, J.S. / Singh, P.K. / Sharma, P. / Kaur, P. / Sharma, S. / Owais, M. / Singh, T.P.
External linksBiochem. J. / PubMed:29301982
MethodsX-ray diffraction
Resolution1.1 - 1.36 Å
Structure data

PDB-5y98:
Crystal structure of native unbound peptidyl tRNA hydrolase from Acinetobacter baumannii at 1.36 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.36 Å

PDB-5y9a:
Crystal structure of the complex of peptidyl tRNA hydrolase with a phosphate ion at the substrate binding site and cytarabine at a new ligand binding site at 1.1 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-AR3:
CYTARABINE / medication, chemotherapy*YM

ChemComp-PO4:
PHOSPHATE ION

Source
  • acinetobacter baumannii (strain atcc 19606 / dsm 30007 / cip 70.34 / jcm 6841 / nbrc 109757 / ncimb 12457 / nctc 12156 / 81) (bacteria)
KeywordsHYDROLASE

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