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- PDB-4op2: GKRP bound to AMG-0471 and Sorbitol-6-Phosphate -

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Basic information

Entry
Database: PDB / ID: 4op2
TitleGKRP bound to AMG-0471 and Sorbitol-6-Phosphate
ComponentsGlucokinase Regulatory Protein
KeywordsCARBOHYDRATE BINDING PROTEIN/INHIBITOR / SIS domain containing protein / Binds to and inhibits Glucokinase / Glucokinase / CARBOHYDRATE BINDING PROTEIN-INHIBITOR complex
Function / homology
Function and homology information


glucose sensor activity / negative regulation of glucokinase activity / fructose-6-phosphate binding / carbohydrate derivative metabolic process / kinase inhibitor activity / urate metabolic process / response to fructose / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / triglyceride homeostasis ...glucose sensor activity / negative regulation of glucokinase activity / fructose-6-phosphate binding / carbohydrate derivative metabolic process / kinase inhibitor activity / urate metabolic process / response to fructose / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / triglyceride homeostasis / intracellular glucose homeostasis / protein localization to nucleus / response to glucose / protein import into nucleus / mitochondrion / nucleoplasm / cytoplasm / cytosol
Similarity search - Function
: / Glucokinase regulatory protein, second SIS domain / Glucokinase regulatory protein, conserved site / N-acetylmuramic acid 6-phosphate etherase/glucokinase regulatory protein / C-terminal lid domain of glucokinase regulatory protein / Glucokinase regulatory protein N-terminal SIS domain / Glucokinase regulatory protein family signature. / SIS domain / SIS domain profile. / SIS domain superfamily ...: / Glucokinase regulatory protein, second SIS domain / Glucokinase regulatory protein, conserved site / N-acetylmuramic acid 6-phosphate etherase/glucokinase regulatory protein / C-terminal lid domain of glucokinase regulatory protein / Glucokinase regulatory protein N-terminal SIS domain / Glucokinase regulatory protein family signature. / SIS domain / SIS domain profile. / SIS domain superfamily / Glucose-6-phosphate isomerase like protein; domain 1 / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-2UX / IODIDE ION / D-SORBITOL-6-PHOSPHATE / Glucokinase regulatory protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.24 Å
AuthorsJordan, S.R. / Chmait, S.
CitationJournal: J.Med.Chem. / Year: 2015
Title: Small Molecule Disruptors of the Glucokinase-Glucokinase Regulatory Protein Interaction: 5. A Novel Aryl Sulfone Series, Optimization Through Conformational Analysis.
Authors: Tamayo, N.A. / Norman, M.H. / Bartberger, M.D. / Hong, F.T. / Bo, Y. / Liu, L. / Nishimura, N. / Yang, K.C. / Tadesse, S. / Fotsch, C. / Chen, J. / Chmait, S. / Cupples, R. / Hale, C. / ...Authors: Tamayo, N.A. / Norman, M.H. / Bartberger, M.D. / Hong, F.T. / Bo, Y. / Liu, L. / Nishimura, N. / Yang, K.C. / Tadesse, S. / Fotsch, C. / Chen, J. / Chmait, S. / Cupples, R. / Hale, C. / Jordan, S.R. / Lloyd, D.J. / Sivits, G. / Van, G. / St Jean, D.J.
History
DepositionFeb 4, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 30, 2014Provider: repository / Type: Initial release
Revision 1.1Jun 24, 2015Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Glucokinase Regulatory Protein
B: Glucokinase Regulatory Protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,66236
Polymers140,6132
Non-polymers5,04934
Water3,225179
1
A: Glucokinase Regulatory Protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,51415
Polymers70,3071
Non-polymers2,20714
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Glucokinase Regulatory Protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,14821
Polymers70,3071
Non-polymers2,84220
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)149.053, 149.053, 131.833
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number170
Space group name H-MP65

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Components

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Protein / Sugars , 2 types, 4 molecules AB

#1: Protein Glucokinase Regulatory Protein / Glucokinase regulator


Mass: 70306.617 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GCKR / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q14397
#3: Sugar ChemComp-S6P / D-SORBITOL-6-PHOSPHATE / 1-O-PHOSPHONO-D-GLUCITOL / D-GLUCITOL-6-PHOSPHATE


Type: D-saccharide / Mass: 262.152 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C6H15O9P

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Non-polymers , 5 types, 211 molecules

#2: Chemical ChemComp-2UX / (2S)-2-{4'-[(6-aminopyridin-3-yl)sulfonyl]biphenyl-4-yl}-1,1,1-trifluoropropan-2-ol


Mass: 422.421 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H17F3N2O3S
#4: Chemical...
ChemComp-IOD / IODIDE ION


Mass: 126.904 Da / Num. of mol.: 26 / Source method: obtained synthetically / Formula: I
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 179 / Source method: isolated from a natural source / Formula: H2O

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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: 3.01 Å3/Da / Density % sol: 59.09 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.1M Bis-tris, 0.2M NaI, 16%PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU FR-E SUPERBRIGHT / Wavelength: 1.5418 Å
DetectorType: RIGAKU SATURN 92 / Detector: CCD / Date: Apr 25, 2011 / Details: mirrors
RadiationMonochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.24→50 Å / Num. all: 76070 / Num. obs: 71470 / % possible obs: 93.9 % / Observed criterion σ(F): 1

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Processing

Software
NameVersionClassification
HKL-2000data collection
AMoREphasing
REFMAC5.8.0049refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4LY9

4ly9


Resolution: 2.24→36.32 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.918 / SU B: 7.057 / SU ML: 0.173 / Cross valid method: THROUGHOUT / ESU R: 0.268 / ESU R Free: 0.228 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27037 3786 5 %RANDOM
Rwork0.2192 ---
obs0.22182 71470 93.89 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 47.628 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å2-0 Å2
3----0.01 Å2
Refinement stepCycle: LAST / Resolution: 2.24→36.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9075 0 137 179 9391
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0199349
X-RAY DIFFRACTIONr_bond_other_d0.0010.029153
X-RAY DIFFRACTIONr_angle_refined_deg1.8491.97912663
X-RAY DIFFRACTIONr_angle_other_deg0.8983.00121010
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.92151169
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.8524.415376
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.825151658
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.7821550
X-RAY DIFFRACTIONr_chiral_restr0.1030.21483
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.02110388
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022038
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it4.0354.5684694
X-RAY DIFFRACTIONr_mcbond_other4.0344.5684693
X-RAY DIFFRACTIONr_mcangle_it5.7416.8325857
X-RAY DIFFRACTIONr_mcangle_other5.7416.8325858
X-RAY DIFFRACTIONr_scbond_it4.3944.9524655
X-RAY DIFFRACTIONr_scbond_other4.3274.9464643
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.3457.2746789
X-RAY DIFFRACTIONr_long_range_B_refined8.4336.49210816
X-RAY DIFFRACTIONr_long_range_B_other8.4336.49410817
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.24→2.294 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.35 195 -
Rwork0.293 3985 -
obs--70.85 %

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