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Yorodumi- PDB-1i8z: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO[3,2-E]-1,2... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1i8z | ||||||
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Title | CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE | ||||||
Components | CARBONIC ANHYDRASE II | ||||||
Keywords | LYASE / Carbonic Anhydrase II / AL-6629 | ||||||
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 / regulation of chloride transport / arylesterase activity / 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 / regulation of chloride transport / arylesterase activity / 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 / extracellular exosome / zinc ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.93 Å | ||||||
Authors | Kim, C.-Y. / Chang, J.S. / Liao, J. / May, J.A. / Christianson, D.W. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2002 Title: Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV. Authors: Kim, C.Y. / Whittington, D.A. / Chang, J.S. / Liao, J. / May, J.A. / Christianson, D.W. | ||||||
History |
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Remark 999 | SEQUENCE THE RESIDUE NUMBERING IS NOT SEQUENTIAL. RESIDUE 125 IS COVALENTLY BOUND TO RESIDUE 127. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i8z.cif.gz | 70 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i8z.ent.gz | 50.7 KB | Display | PDB format |
PDBx/mmJSON format | 1i8z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1i8z_validation.pdf.gz | 453.7 KB | Display | wwPDB validaton report |
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Full document | 1i8z_full_validation.pdf.gz | 460.6 KB | Display | |
Data in XML | 1i8z_validation.xml.gz | 8 KB | Display | |
Data in CIF | 1i8z_validation.cif.gz | 12.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i8/1i8z ftp://data.pdbj.org/pub/pdb/validation_reports/i8/1i8z | HTTPS FTP |
-Related 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: 29157.863 Da / Num. of mol.: 1 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-INL / |
#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: 2.22 Å3/Da / Density % sol: 44.69 % | ||||||||||||||||||||||||||||||||||||
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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 ℃ | ||||||||||||||||||||||||||||||||||||
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: Dec 17, 1998 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.93→20 Å / Num. all: 19173 / Num. obs: 19173 / % possible obs: 93.6 % / Observed criterion σ(F): 2 / Redundancy: 6.2 % / Biso Wilson estimate: 18.47 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 13.4 |
Reflection shell | Resolution: 1.93→2 Å / Rmerge(I) obs: 0.237 / % possible all: 89.8 |
Reflection | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 20 Å / Num. obs: 16912 / % possible obs: 99.1 % / Num. measured all: 54642 / Rmerge(I) obs: 0.105 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 1.93→20 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.93→20 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.1 Å / Num. reflection obs: 15740 / σ(F): 2 / Num. reflection Rfree: 767 / Rfactor obs: 0.155 / Rfactor Rfree: 0.208 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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