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Structure paper

TitleA synthetic protein selected for ligand binding affinity mediates ATP hydrolysis.
Journal, issue, pagesAcs Chem. Biol., Vol. 4, Page 649-658, Year 2009
Publish dateJun 13, 2008 (structure data deposition date)
AuthorsSimmons, C.R. / Stomel, J.M. / McConnell, M.D. / Smith, D.A. / Watkins, J.L. / Allen, J.P. / Chaput, J.C.
External linksAcs Chem. Biol. / PubMed:19522480
MethodsX-ray diffraction
Resolution1.8 - 2.7 Å
Structure data

PDB-3dgl:
1.8 A Crystal Structure of a Non-biological Protein with Bound ATP in a Novel Bent Conformation
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3dgn:
A non-biological ATP binding protein crystallized in the presence of 100 mM ADP
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3dgo:
A non-biological ATP binding protein with a Tyr-Phe mutation in the ligand binding domain
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-CL:
Unknown entry

Source
  • unidentified (others)
KeywordsDE NOVO PROTEIN / alpha/beta fold / bent ATP / non-biological protein

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