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- PDB-9psx: Q108K:K40L:T51V:T53S:R58W:Y19W:L117E mutant of hCRBPII bound to f... -

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Basic information

Entry
Database: PDB / ID: 9psx
TitleQ108K:K40L:T51V:T53S:R58W:Y19W:L117E mutant of hCRBPII bound to fluorophore TD-1V-3
ComponentsRetinol-binding protein 2
KeywordsRETINOL BINDING PROTEIN / human cellular retinol binding protein II / hCRBPII / fluorescent protein / engineered protein
Function / homology
Function and homology information


vitamin A metabolic process / molecular carrier activity / retinoid binding / retinal binding / retinol binding / epidermis development / fatty acid transport / Retinoid metabolism and transport / fatty acid binding / nucleus / cytosol
Similarity search - Function
Cytosolic fatty-acid binding proteins signature. / Intracellular lipid binding protein / Cytosolic fatty-acid binding / Lipocalin / cytosolic fatty-acid binding protein family / Lipocalin/cytosolic fatty-acid binding domain / Calycin
Similarity search - Domain/homology
: / ACETATE ION / Retinol-binding protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.29 Å
AuthorsGhanbarpour, A. / Bingham, C. / Geiger, J.H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Biomedical Imaging and Bioengineering (NIH/NIBIB) United States
CitationJournal: To Be Published
Title: Exploring the Structure-Property Relationships of Protein/Fluorophore Complex
Authors: Santos, E. / Ghanbarpour, A. / Chandra, I. / Bingham, C. / Vasileiou, C. / Geiger, J.H. / Borhan, B.
History
DepositionJul 27, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 29, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Retinol-binding protein 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)16,0134
Polymers15,6361
Non-polymers3763
Water3,855214
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area450 Å2
ΔGint-2 kcal/mol
Surface area7010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)29.541, 66.450, 63.861
Angle α, β, γ (deg.)90.000, 90.384, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z
Components on special symmetry positions
IDModelComponents
11A-443-

HOH

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Components

#1: Protein Retinol-binding protein 2 / Cellular retinol-binding protein II / CRBP-II


Mass: 15636.464 Da / Num. of mol.: 1 / Mutation: Q108K:K40L:T51V:T53S:R58W:Y19W:L117E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBP2, CRBP2 / Production host: Escherichia coli (E. coli) / References: UniProt: P50120
#2: Chemical ChemComp-A1CKW / (2E)-3-[5-(4-methoxyphenyl)thiophen-2-yl]but-2-enal


Mass: 258.335 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C15H14O2S / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 214 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2 Å3/Da / Density % sol: 38.63 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: PEG4000, ammonium acetate, 100 mM sodium acetate, pH 4.0 - 4.8

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 1.127 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Dec 19, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.127 Å / Relative weight: 1
ReflectionResolution: 1.28→29.47 Å / Num. obs: 30407 / % possible obs: 96.91 % / Redundancy: 2.7 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 17.2
Reflection shellResolution: 1.28→1.33 Å / Rmerge(I) obs: 0.534 / Num. unique obs: 2898

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Processing

Software
NameVersionClassification
PHENIX1.21.2_5419refinement
Cootmodel building
HKL-2000data scaling
PHASERphasing
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.29→29.47 Å / SU ML: 0.1058 / Cross valid method: FREE R-VALUE / σ(F): 1.43 / Phase error: 18.1804
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1864 1970 6.59 %
Rwork0.1743 27916 -
obs0.1751 29886 95.29 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 13.99 Å2
Refinement stepCycle: LAST / Resolution: 1.29→29.47 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1099 0 25 214 1338
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01161150
X-RAY DIFFRACTIONf_angle_d1.18881550
X-RAY DIFFRACTIONf_chiral_restr0.4072162
X-RAY DIFFRACTIONf_plane_restr0.0056199
X-RAY DIFFRACTIONf_dihedral_angle_d25.5967415
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.29-1.320.19681220.22111803X-RAY DIFFRACTION87.58
1.32-1.350.23551430.2141995X-RAY DIFFRACTION94.19
1.35-1.390.22521360.2111973X-RAY DIFFRACTION95.26
1.39-1.440.21621420.21041980X-RAY DIFFRACTION95.41
1.44-1.490.21051430.19681990X-RAY DIFFRACTION95.39
1.49-1.550.19991360.18442000X-RAY DIFFRACTION96.17
1.55-1.620.20221390.18482034X-RAY DIFFRACTION96.75
1.62-1.70.1761430.18062023X-RAY DIFFRACTION96.96
1.7-1.810.22141420.1882011X-RAY DIFFRACTION96.03
1.81-1.950.20751340.17641814X-RAY DIFFRACTION87.32
1.95-2.150.17891390.16831987X-RAY DIFFRACTION93.95
2.15-2.460.19371500.1722087X-RAY DIFFRACTION99.73
2.46-3.10.17621480.1792083X-RAY DIFFRACTION99.69
3.1-29.470.15481530.14362136X-RAY DIFFRACTION99.57

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