+Open data
-Basic information
Entry | Database: PDB / ID: 1yo1 | ||||||
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Title | Proton Transfer from His200 in Human Carbonic Anhydrase II | ||||||
Components | Carbonic anhydrase II | ||||||
Keywords | LYASE / proton transfer human carbonic anhydrase | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Bhatt, D. / Tu, C. / Fisher, S.Z. / Hernandez Prada, J.A. / McKenna, R. / Silverman, D.N. | ||||||
Citation | Journal: Proteins / Year: 2005 Title: Proton transfer in a Thr200His mutant of human carbonic anhydrase II Authors: Bhatt, D. / Tu, C. / Fisher, S.Z. / Hernandez Prada, J.A. / McKenna, R. / Silverman, D.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1yo1.cif.gz | 67.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1yo1.ent.gz | 48.1 KB | Display | PDB format |
PDBx/mmJSON format | 1yo1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yo/1yo1 ftp://data.pdbj.org/pub/pdb/validation_reports/yo/1yo1 | HTTPS FTP |
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-Related structure data
Related structure data | 1yo0C 1yo2C 2cbaS C: citing same article (ref.) S: Starting model for refinement |
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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: 29259.035 Da / Num. of mol.: 1 / Mutation: H63A, T199H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CA2 / Plasmid: pET31 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P00918, carbonic anhydrase |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-ZN / |
#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: 2.13 Å3/Da / Density % sol: 42.28 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 50 mM Tris-Cl, 2.5 M AmmSO4, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Details: Osmic Mirror |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. all: 27359 / Num. obs: 25688 / % possible obs: 93.5 % / Rsym value: 0.056 |
Reflection shell | Resolution: 1.7→1.76 Å / Num. unique all: 2391 / Rsym value: 0.308 / % possible all: 88.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 2CBA Resolution: 1.7→20 Å / Cross valid method: random / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→20 Å
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Refine LS restraints |
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