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Yorodumi- PDB-1fsq: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/W97M CARBONIC A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fsq | ||||||
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Title | X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT | ||||||
Components | CARBONIC ANHYDRASE II | ||||||
Keywords | LYASE / carbonic anhydrase / metal binding / metal specificity / cobalt | ||||||
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 / Resolution: 2 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 | 1fsq.cif.gz | 115.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fsq.ent.gz | 88.9 KB | Display | PDB format |
PDBx/mmJSON format | 1fsq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fsq_validation.pdf.gz | 370 KB | Display | wwPDB validaton report |
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Full document | 1fsq_full_validation.pdf.gz | 381.1 KB | Display | |
Data in XML | 1fsq_validation.xml.gz | 12.2 KB | Display | |
Data in CIF | 1fsq_validation.cif.gz | 17.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/1fsq ftp://data.pdbj.org/pub/pdb/validation_reports/fs/1fsq | HTTPS FTP |
-Related structure data
Related structure data | 1fqlC 1fqmC 1fqnC 1fqrC 1fr4C 1fr7C 1fsnC 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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2 |
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Unit cell |
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Details | The biological assembly is a monomer |
-Components
#1: Protein | Mass: 29139.934 Da / Num. of mol.: 2 / Mutation: F93S/F95L/W97M 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 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 39.86 % | ||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7 Details: HEPES, PEG 1500, pH 7.0, 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: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Dec 6, 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: 2→20 Å / Num. all: 31561 / Num. obs: 29510 / % possible obs: 93.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 1.8 % / Biso Wilson estimate: 20.4 Å2 / Rmerge(I) obs: 0.057 / Net I/σ(I): 7 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.228 / % possible all: 78.2 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / Num. measured all: 52591 |
Reflection shell | *PLUS % possible obs: 78.2 % |
-Processing
Software |
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Refinement | Resolution: 2→20 Å / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→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: 2 Å / Lowest resolution: 20 Å / σ(F): 2 / Rfactor Rfree: 0.25 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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