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- PDB-5v4w: Human glucokinase in complex with novel indazole activator. -

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Basic information

Entry
Database: PDB / ID: 5v4w
TitleHuman glucokinase in complex with novel indazole activator.
ComponentsGlucokinase
Keywordstransferase/transferase activator / activator / complex / allosteric / transferase-transferase activator complex
Function / homology
Function and homology information


Defective GCK causes maturity-onset diabetes of the young 2 (MODY2) / detection of glucose / regulation of potassium ion transport / mannokinase activity / hexokinase / fructokinase activity / glucokinase activity / canonical glycolysis / glucose 6-phosphate metabolic process / NADP metabolic process ...Defective GCK causes maturity-onset diabetes of the young 2 (MODY2) / detection of glucose / regulation of potassium ion transport / mannokinase activity / hexokinase / fructokinase activity / glucokinase activity / canonical glycolysis / glucose 6-phosphate metabolic process / NADP metabolic process / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Regulation of Glucokinase by Glucokinase Regulatory Protein / glucose binding / cellular response to leptin stimulus / calcium ion import / regulation of glycolytic process / Glycolysis / cellular glucose homeostasis / Regulation of gene expression in beta cells / regulation of insulin secretion / positive regulation of insulin secretion / negative regulation of gluconeogenesis / positive regulation of glycogen biosynthetic process / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / glycolytic process / cellular response to insulin stimulus / glucose homeostasis / mitochondrion / nucleoplasm / ATP binding / cytosol
Similarity search - Function
Hexokinase-4, chordate / Hexokinase; domain 1 / Hexokinase; domain 1 - #20 / Hexokinase, N-terminal / Hexokinase domain signature. / Hexokinase, binding site / Hexokinase / Hexokinase / Hexokinase, C-terminal / Hexokinase ...Hexokinase-4, chordate / Hexokinase; domain 1 / Hexokinase; domain 1 - #20 / Hexokinase, N-terminal / Hexokinase domain signature. / Hexokinase, binding site / Hexokinase / Hexokinase / Hexokinase, C-terminal / Hexokinase / Hexokinase domain profile. / ATPase, nucleotide binding domain / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-8WM / alpha-D-glucopyranose / IODIDE ION / Hexokinase-4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.39 Å
AuthorsSkene, R.J. / Hosfield, D.J.
CitationJournal: Bioorg. Med. Chem. Lett. / Year: 2017
Title: Discovery of potent and orally active 1,4-disubstituted indazoles as novel allosteric glucokinase activators.
Authors: Cheruvallath, Z.S. / Gwaltney, S.L. / Sabat, M. / Tang, M. / Wang, H. / Jennings, A. / Hosfield, D. / Lee, B. / Wu, Y. / Halkowycz, P. / Grimshaw, C.E.
History
DepositionMar 10, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 31, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 7, 2017Group: Database references
Revision 1.2Nov 22, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Glucokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)52,1614
Polymers51,3751
Non-polymers7863
Water4,053225
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)49.709, 78.873, 120.333
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Glucokinase / / Hexokinase type IV / HK IV / Hexokinase-4 / HK4 / Hexokinase-D


Mass: 51375.328 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GCK / Production host: Escherichia coli (E. coli) / References: UniProt: P35557, glucokinase
#2: Sugar ChemComp-GLC / alpha-D-glucopyranose / Glucose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DGlcpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-glucopyranoseCOMMON NAMEGMML 1.0
a-D-GlcpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Chemical ChemComp-8WM / (2S)-2-[4-(cyclopropylsulfonyl)-1H-indazol-1-yl]-N-(5-fluoro-1,3-thiazol-2-yl)-3-(oxan-4-yl)propanamide


Mass: 478.560 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H23FN4O4S2
#4: Chemical ChemComp-IOD / IODIDE ION / Iodide


Mass: 126.904 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: I
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 225 / 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: 2.3 Å3/Da / Density % sol: 46.42 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 15% PEG3350, 200 mM ammonium iodide, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1.594 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 28, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.594 Å / Relative weight: 1
ReflectionResolution: 2.4→65.94 Å / Num. obs: 19113 / % possible obs: 99.1 % / Redundancy: 5.8 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 9.1
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.458 / % possible all: 89.6

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Processing

Software
NameVersionClassification
REFMACrefinement
HKL-2000data scaling
PDB_EXTRACT3.22data extraction
HKL-2000data reduction
MOLREPphasing
DENZOdata reduction
SCALEPACKdata scaling
RefinementResolution: 2.39→65.94 Å / SU B: 16.293 / SU ML: 0.206 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.47 / ESU R Free: 0.284
RfactorNum. reflection% reflectionSelection details
Rfree0.261 978 5.1 %RANDOM
Rwork0.198 ---
obs0.201 18071 98.8 %-
Displacement parametersBiso mean: 30.88 Å2
Baniso -1Baniso -2Baniso -3
1-0.43 Å20 Å20 Å2
2--0.21 Å20 Å2
3----0.64 Å2
Refinement stepCycle: LAST / Resolution: 2.39→65.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3276 0 45 225 3546

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