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Yorodumi- PDB-1fr4: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/W97V CARBONIC A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fr4 | ||||||
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Title | X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT | ||||||
Components | CARBONIC ANHYDRASE IICarbonic anhydrase | ||||||
Keywords | LYASE / carbonic anhydrase / metal binding / metal specificity / copper | ||||||
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 / regulation of intracellular pH / morphogenesis of an epithelium / 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 / SYNCHROTRON / Resolution: 1.6 Å | ||||||
Authors | Cox, J.D. / Hunt, J.A. / Compher, K.M. / Fierke, C.A. / Christianson, D.W. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II. Authors: Cox, J.D. / Hunt, J.A. / Compher, K.M. / Fierke, C.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 | 1fr4.cif.gz | 64.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fr4.ent.gz | 47 KB | Display | PDB format |
PDBx/mmJSON format | 1fr4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fr/1fr4 ftp://data.pdbj.org/pub/pdb/validation_reports/fr/1fr4 | HTTPS FTP |
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-Related structure data
Related structure data | 1fqlC 1fqmC 1fqnC 1fqrC 1fr7C 1fsnC 1fsqC 1fsrC 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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Details | The biological assembly is a monomer |
-Components
#1: Protein | Mass: 29151.984 Da / Num. of mol.: 1 / Mutation: F93I/F95M/W97V 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-CU / |
#3: Chemical | ChemComp-SO4 / |
#4: 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: 2.08 Å3/Da / Density % sol: 40.95 % | ||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: ammonium sulfate, tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12B / Wavelength: 0.978 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 27, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20 Å / Num. all: 32173 / Num. obs: 31111 / % possible obs: 96.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Biso Wilson estimate: 19.5 Å2 / Rmerge(I) obs: 0.048 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.298 / % possible all: 76.2 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 80681 |
Reflection shell | *PLUS % possible obs: 76.2 % |
-Processing
Software |
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Refinement | Resolution: 1.6→20 Å / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.6→20 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 20 Å / σ(F): 2 / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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