+Open data
-Basic information
Entry | Database: PDB / ID: 4iw1 | ||||||
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Title | HSA-fructose complex | ||||||
Components | Serum albumin | ||||||
Keywords | TRANSPORT PROTEIN / Heart shape / transport | ||||||
Function / homology | Function and homology information cellular response to calcium ion starvation / exogenous protein binding / Ciprofloxacin ADME / HDL remodeling / enterobactin binding / Heme biosynthesis / negative regulation of mitochondrial depolarization / Prednisone ADME / Heme degradation / antioxidant activity ...cellular response to calcium ion starvation / exogenous protein binding / Ciprofloxacin ADME / HDL remodeling / enterobactin binding / Heme biosynthesis / negative regulation of mitochondrial depolarization / Prednisone ADME / Heme degradation / antioxidant activity / Aspirin ADME / toxic substance binding / Scavenging of heme from plasma / Recycling of bile acids and salts / cellular response to starvation / platelet alpha granule lumen / fatty acid binding / Post-translational protein phosphorylation / Cytoprotection by HMOX1 / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / pyridoxal phosphate binding / Platelet degranulation / protein-folding chaperone binding / blood microparticle / copper ion binding / endoplasmic reticulum lumen / Golgi apparatus / endoplasmic reticulum / protein-containing complex / DNA binding / extracellular space / extracellular exosome / extracellular region / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.56 Å | ||||||
Authors | Wang, Y. / Yu, H. / Shi, X. / Huang, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2013 Title: Structural mechanism of ring-opening reaction of glucose by human serum albumin Authors: Wang, Y. / Yu, H. / Shi, X. / Luo, Z. / Lin, D. / Huang, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4iw1.cif.gz | 122 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4iw1.ent.gz | 92.8 KB | Display | PDB format |
PDBx/mmJSON format | 4iw1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iw/4iw1 ftp://data.pdbj.org/pub/pdb/validation_reports/iw/4iw1 | HTTPS FTP |
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-Related structure data
Related structure data | 4iw2C 4k2cC 1ao6S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 66571.219 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ALB / Production host: Pichia pastoris (fungus) / References: UniProt: P02768 |
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#2: Sugar | ChemComp-FRU / |
#3: Chemical | ChemComp-PO4 / |
#4: Sugar | ChemComp-FUD / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.92 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.4 Details: 25%-30% PEG 3350, 50mM potassium phosphate, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Dec 10, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.56→50 Å / Num. all: 18509 / Num. obs: 18509 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1AO6 Resolution: 2.56→48.41 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.88 / SU B: 18.162 / SU ML: 0.388 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / ESU R: 2.587 / ESU R Free: 0.411 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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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: 60.638 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.56→48.41 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.555→2.621 Å / Total num. of bins used: 20
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Xplor file |
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