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Yorodumi- PDB-1e7h: HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID) -
+Open data
-Basic information
Entry | Database: PDB / ID: 1e7h | ||||||
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Title | HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID) | ||||||
Components | SERUM ALBUMIN | ||||||
Keywords | PLASMA PROTEIN / METAL-BINDING / LIPID-BINDING | ||||||
Function / homology | Function and homology information cellular response to calcium ion starvation / exogenous protein binding / Ciprofloxacin ADME / enterobactin binding / Heme biosynthesis / HDL remodeling / negative regulation of mitochondrial depolarization / Prednisone ADME / Heme degradation / Aspirin ADME ...cellular response to calcium ion starvation / exogenous protein binding / Ciprofloxacin ADME / enterobactin binding / Heme biosynthesis / HDL remodeling / negative regulation of mitochondrial depolarization / Prednisone ADME / Heme degradation / Aspirin ADME / antioxidant activity / 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: 2.43 Å | ||||||
Authors | Bhattacharya, A.A. / Gruene, T. / Curry, S. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Crystallographic Analysis Reveals Common Modes of Binding of Medium and Long-Chain Fatty Acids to Human Serum Albumin Authors: Bhattacharya, A.A. / Grune, T. / Curry, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e7h.cif.gz | 127.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e7h.ent.gz | 98 KB | Display | PDB format |
PDBx/mmJSON format | 1e7h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1e7h_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 1e7h_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 1e7h_validation.xml.gz | 25.1 KB | Display | |
Data in CIF | 1e7h_validation.cif.gz | 33.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e7/1e7h ftp://data.pdbj.org/pub/pdb/validation_reports/e7/1e7h | HTTPS FTP |
-Related structure data
Related structure data | 1e7eC 1e7fC 1e7gC 1e7iC 1bj5S S: Starting model for refinement C: citing same article (ref.) |
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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) / Cellular location: SERUM / Gene: ALB / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast) / References: UniProt: P02768 | ||||||
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#2: Chemical | ChemComp-PLM / #3: Water | ChemComp-HOH / | Compound details | SERUM ALBUMIN, REGULATES THE COLLOIDAL OSMOTIC PRESSURE OF BLOOD IT BINDS TO WATER, CA++, NA+, K+, ...SERUM ALBUMIN, REGULATES THE COLLOIDAL OSMOTIC PRESSURE OF BLOOD IT BINDS TO WATER, CA++, NA+, K+, FATTY ACIDS, HORMONES, BILIRUBIN AND DRUGS | Sequence details | 1BJ5 SWS P02768 1 - 26 NOT IN ATOMS LIST 1BJ5 SWS P02768 609 - 609 NOT IN ATOMS LIST | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 54 % | ||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.00 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop / Details: Curry, S., (1998) Nature Struct. Biol., 5, 827. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 0.87 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1998 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.44→11.99 Å / Num. obs: 24122 / % possible obs: 92.9 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Biso Wilson estimate: 34.5 Å2 / Rmerge(I) obs: 0.046 / Rsym value: 0.046 / Net I/σ(I): 9.4 |
Reflection shell | Resolution: 2.44→2.57 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.178 / Mean I/σ(I) obs: 4 / Rsym value: 0.178 / % possible all: 87.8 |
Reflection shell | *PLUS % possible obs: 87.8 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1BJ5 Resolution: 2.43→12 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: BULK SOLVENT MODEL USED RESIDUES ASP 1, ALA 2, GLY 584 AND LEU 585 ARE DISORDERED AND HAVE NOT BEEN INCLUDED IN THE MODEL.
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Displacement parameters | Biso mean: 51.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.43→12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.43→2.54 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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