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TitleStructures of holo wild-type human cellular retinol-binding protein II (hCRBPII) bound to retinol and retinal.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 3226-3232, Year 2014
Publish dateJul 24, 2014 (structure data deposition date)
AuthorsNossoni, Z. / Assar, Z. / Yapici, I. / Nosrati, M. / Wang, W. / Berbasova, T. / Vasileiou, C. / Borhan, B. / Geiger, J.
External linksActa Crystallogr. ,Sect. D / PubMed:25478840
MethodsX-ray diffraction
Resolution1.19 - 1.9 Å
Structure data

PDB-4qyn:
The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinol
Method: X-RAY DIFFRACTION / Resolution: 1.19 Å

PDB-4qyp:
The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinal
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

PDB-4qzt:
Crystal Structure of wild type Human Cellular Retinol Binding Protein II (hCRBPII) bound to retinol at 7 KeV beam energy
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4qzu:
Crystal Structure of wild type Human Cellular Retinol Binding Protein II (hCRBPII) bound to retinol at 11 KeV beam energy
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-RTL:
RETINOL

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-RET:
RETINAL

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / beta barrel / transfer protein / kidney / lover / liver / RETINOL-BINDING PROT / PROTEIN BINDING / Retinol / Human Cellular Retinol Binding Protein II / intracellular lipid binding protein / X-ray flux / X-ray damage / Retinal / Retinoid Chaperones

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