+Open data
-Basic information
Entry | Database: PDB / ID: 4mqu | ||||||
---|---|---|---|---|---|---|---|
Title | Human GKRP complexed to AMG-3969 and S6P | ||||||
Components | Glucokinase regulatory protein | ||||||
Keywords | Transferase Inhibitor / SIS domains / Regulatory protein / Binds fructose phosphates and glucokinase | ||||||
Function / homology | Function and homology information amino sugar catabolic process / ether hydrolase activity / carbon-oxygen lyase activity / negative regulation of glucokinase activity / glucose sensor activity / fructose-6-phosphate binding / urate metabolic process / kinase inhibitor activity / peptidoglycan turnover / Regulation of Glucokinase by Glucokinase Regulatory Protein ...amino sugar catabolic process / ether hydrolase activity / carbon-oxygen lyase activity / negative regulation of glucokinase activity / glucose sensor activity / fructose-6-phosphate binding / urate metabolic process / kinase inhibitor activity / peptidoglycan turnover / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / response to fructose / triglyceride homeostasis / enzyme inhibitor activity / response to glucose / protein import into nucleus / glucose homeostasis / carbohydrate binding / enzyme binding / mitochondrion / nucleoplasm / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.22 Å | ||||||
Authors | St Jean, D.J. / Ashton, K.S. / Bartberger, M.D. / Chen, J. / Chmait, S. / Cupples, R. / Galbreath, E. / Helmering, J. / Jordan, S.R. / Liu, L. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2014 Title: Small molecule disruptors of the glucokinase-glucokinase regulatory protein interaction: 2. Leveraging structure-based drug design to identify analogues with improved pharmacokinetic profiles. Authors: St Jean, D.J. / Ashton, K.S. / Bartberger, M.D. / Chen, J. / Chmait, S. / Cupples, R. / Galbreath, E. / Helmering, J. / Hong, F.T. / Jordan, S.R. / Liu, L. / Kunz, R.K. / Michelsen, K. / ...Authors: St Jean, D.J. / Ashton, K.S. / Bartberger, M.D. / Chen, J. / Chmait, S. / Cupples, R. / Galbreath, E. / Helmering, J. / Hong, F.T. / Jordan, S.R. / Liu, L. / Kunz, R.K. / Michelsen, K. / Nishimura, N. / Pennington, L.D. / Poon, S.F. / Reid, D. / Sivits, G. / Stec, M.M. / Tadesse, S. / Tamayo, N. / Van, G. / Yang, K.C. / Zhang, J. / Norman, M.H. / Fotsch, C. / Lloyd, D.J. / Hale, C. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4mqu.cif.gz | 243.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4mqu.ent.gz | 195.3 KB | Display | PDB format |
PDBx/mmJSON format | 4mqu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mq/4mqu ftp://data.pdbj.org/pub/pdb/validation_reports/mq/4mqu | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
-Protein / Sugars , 2 types, 4 molecules AB
#1: Protein | Mass: 70178.492 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 | |
---|
-Non-polymers , 5 types, 264 molecules
#2: Chemical | #4: Chemical | ChemComp-IOD / #5: Chemical | ChemComp-GOL / | #6: Chemical | #7: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.36 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Well buffer: 0.1M Bis-tris, 0.2M NaI, 16% PEG 8K, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E DW |
Detector | Type: RIGAKU SATURN 92 / Detector: CCD |
Radiation | Monochromator: Confocal mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.2→35.8 Å / Num. all: 62711 / Num. obs: 58853 / % possible obs: 93.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Internal structures Resolution: 2.22→35.8 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.909 / SU B: 7.408 / SU ML: 0.181 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.354 / ESU R Free: 0.275 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.458 Å2
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.22→35.8 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.219→2.277 Å / Total num. of bins used: 20
|