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IF

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Structure paper

TitleEvidence for dynamics in proteins as a mechanism for ligand dissociation.
Journal, issue, pagesNat. Chem. Biol., Vol. 8, Page 246-252, Year 2012
Publish dateMar 3, 2011 (structure data deposition date)
AuthorsCarroll, M.J. / Mauldin, R.V. / Gromova, A.V. / Singleton, S.F. / Collins, E.J. / Lee, A.L.
External linksNat. Chem. Biol. / PubMed:22246400
MethodsX-ray diffraction
Resolution1.79 - 2.09 Å
Structure data

PDB-3qyl:
Sensitivity of receptor internal motions to ligand binding affinity and kinetic off-rate
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-3qyo:
Sensitivity of receptor internal motions to ligand binding affinity and kinetic off-rate
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-3r33:
Evidence for dynamic motion in proteins as a mechanism for ligand dissociation
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

Chemicals

ChemComp-7ME:
(7S)-7-methyl-5,6,7,8-tetrahydroquinazoline-2,4-diamine

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-Q24:
quinazoline-2,4-diamine

ChemComp-6ME:
(6S)-6-methyl-5,6,7,8-tetrahydroquinazoline-2,4-diamine

Source
  • escherichia coli k-12 (bacteria)
KeywordsOXIDOREDUCTASE / Rossmann fold / reductase

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