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Yorodumi- PDB-1g46: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1g46 | ||||||
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Title | CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE | ||||||
Components | CARBONIC ANHYDRASE II | ||||||
Keywords | LYASE / Carbonic Anhydrase II / F131V / 4-(aminosulfonyl)-N-[(2 / 3-difluorophenyl)methyl]-benzamide | ||||||
Function / homology | Function and homology information positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / angiotensin-activated signaling pathway ...positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / angiotensin-activated signaling pathway / positive regulation of synaptic transmission, GABAergic / morphogenesis of an epithelium / regulation of intracellular pH / carbonic anhydrase / carbonate dehydratase activity / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / neuron cellular homeostasis / one-carbon metabolic process / apical part of cell / myelin sheath / zinc ion binding / extracellular exosome / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.84 Å | ||||||
Authors | Kim, C.-Y. / Chang, J.S. / Doyon, J.B. / Baird Jr., T.T. / Fierke, C.A. / Jain, A. / Christianson, D.W. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2000 Title: Contribution of Flourine to Protein-ligand Affinity in the Binding of Flouroaromatic Inhibitors to Carbonic Anhydrase II Authors: Kim, C.-Y. / Chang, J.S. / Doyon, J.B. / Baird Jr., T.T. / Fierke, C.A. / Jain, A. / Christianson, D.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g46.cif.gz | 68.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g46.ent.gz | 49.1 KB | Display | PDB format |
PDBx/mmJSON format | 1g46.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1g46_validation.pdf.gz | 442.1 KB | Display | wwPDB validaton report |
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Full document | 1g46_full_validation.pdf.gz | 445.4 KB | Display | |
Data in XML | 1g46_validation.xml.gz | 7.4 KB | Display | |
Data in CIF | 1g46_validation.cif.gz | 11.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g4/1g46 ftp://data.pdbj.org/pub/pdb/validation_reports/g4/1g46 | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 29109.820 Da / Num. of mol.: 1 / Mutation: F131V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P00918, carbonic anhydrase |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-HG / |
#4: Chemical | ChemComp-F2B / |
#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: 2.17 Å3/Da / Density % sol: 43.26 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: methyl mercuric acetate, tris-sulfate, ammonium sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃Details: drop consists of equal amounts of protein and precipitant solutions | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 13, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.84→20 Å / Num. all: 19837 / Num. obs: 18870 / Observed criterion σ(I): -4 / Rmerge(I) obs: 0.082 |
Reflection | *PLUS % possible obs: 94.1 % |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 1.84→20 Å / σ(I): 2
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Refinement step | Cycle: LAST / Resolution: 1.84→20 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||
Refine LS restraints | *PLUS
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