+Open data
-Basic information
Entry | Database: PDB / ID: 3hs4 | ||||||
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Title | Human carbonic anhydrase II complexed with acetazolamide | ||||||
Components | Carbonic anhydrase 2 | ||||||
Keywords | LYASE / Carbonic anhydrase 2 / Carbonic anhydrase II / CA II / CA 2 / Acetazolamide / 5-ACETAMIDO-1 / 3 / 4-THIADIAZOLE-2-SULFONAMIDE / Disease mutation / Metal-binding | ||||||
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 / 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: 1.1 Å | ||||||
Authors | Robbins, A.H. / Genis, C. / Domsic, J. / Sippel, K.H. / Agbandje-McKenna, M. / McKenna, R. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.F / Year: 2009 Title: High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design. Authors: Sippel, K.H. / Robbins, A.H. / Domsic, J. / Genis, C. / Agbandje-McKenna, M. / McKenna, R. #1: Journal: Int.J.Biol.Macromol. / Year: 1990 Title: Refined structure of the acetazolamide complex of human carbonic anhydrase II at 1.9 A. Authors: Vidgren, J. / Liljas, A. / Walker, N.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3hs4.cif.gz | 135.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3hs4.ent.gz | 103 KB | Display | PDB format |
PDBx/mmJSON format | 3hs4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hs/3hs4 ftp://data.pdbj.org/pub/pdb/validation_reports/hs/3hs4 | HTTPS FTP |
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-Related structure data
Related structure data | 2iliS 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: 29289.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CA2 / 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-GOL / | ||
#4: Chemical | #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: 2.06 Å3/Da / Density % sol: 40.37 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 9 Details: 1.3 M Sodium citrate, 100 mM Tris-HCl pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.997 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 10, 2006 / Details: Mirrors |
Radiation | Monochromator: Asymmetric cut Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.997 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→50 Å / Num. all: 98886 / Num. obs: 92557 / % possible obs: 93.6 % / Observed criterion σ(I): 5 / Redundancy: 2.9 % / Biso Wilson estimate: 10.63 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 1.1→1.14 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.303 / Mean I/σ(I) obs: 3.3 / Num. unique all: 7953 / % possible all: 81 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 2ILI Resolution: 1.1→50 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: Used conjugate gradient least squares procedure.
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Displacement parameters | Biso mean: 15.7 Å2 | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→50 Å
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Refine LS restraints |
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LS refinement shell |
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