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Yorodumi- PDB-1moo: Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at hig... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1moo | ||||||
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Title | Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution | ||||||
Components | Carbonic Anhydrase IICarbonic anhydrase | ||||||
Keywords | LYASE / High-resolution / 4-methylimidazole / Twisted Beta Sheet / Zinc Metalloenzyme | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 1.05 Å | ||||||
Authors | Duda, D.M. / Govindasamy, L. / Agbandje-McKenna, M. / Tu, C.K. / Silverman, D.N. / McKenna, R. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2003 Title: The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer. Authors: Duda, D. / Govindasamy, L. / Agbandje-McKenna, M. / Tu, C. / Silverman, D.N. / McKenna, R. #1: Journal: Biochemistry / Year: 2001 Title: Structural and Kinetic Analysis of the Chemical Rescue of the Proton Transfer Function of Carbonic Anhydrase II Authors: Duda, D. / Tu, C.K. / Qian, M. / Laipis, P.J. / Agbandje-McKenna, M. / Silverman, D.N. / McKenna, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1moo.cif.gz | 122.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1moo.ent.gz | 93.3 KB | Display | PDB format |
PDBx/mmJSON format | 1moo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mo/1moo ftp://data.pdbj.org/pub/pdb/validation_reports/mo/1moo | HTTPS FTP |
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-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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Details | The biological assembly is a monomer |
-Components
#1: Protein | Mass: 29221.992 Da / Num. of mol.: 1 / Mutation: H64A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P00918, carbonic anhydrase | ||
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#2: Chemical | ChemComp-ZN / | ||
#3: Chemical | ChemComp-HG / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.07 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: Ammonium Sulfate, Tris, Mercury Chloride, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystal grow | *PLUS Details: Duda, D., (2001) Protein Pept. Lett., 8, 63. |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation | Monochromator: 0.3mm / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.05→20 Å / Num. obs: 112535 / % possible obs: 83.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.106 | ||||||||||||||||||
Reflection | *PLUS Num. obs: 93527 | ||||||||||||||||||
Reflection shell | *PLUS Highest resolution: 1.05 Å / Lowest resolution: 1.09 Å / % possible obs: 40.6 % / Num. unique obs: 4547 / Rmerge(I) obs: 0.316 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.05→20 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refine analyze | Luzzati coordinate error obs: 0.07 Å | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.05→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.05→1.09 Å
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Refinement | *PLUS σ(F): 2 / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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