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Open data
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Basic information
Entry | Database: PDB / ID: 1oq5 | ||||||
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Title | CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR | ||||||
![]() | Carbonic anhydrase II | ||||||
![]() | METAL BINDING PROTEIN / 10-stranded / twisted beta-sheet | ||||||
Function / homology | ![]() 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Weber, A. / Casini, A. / Heine, A. / Kuhn, D. / Supuran, C.T. / Scozzafava, A. / Klebe, G. | ||||||
![]() | ![]() Title: Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition. Authors: Weber, A. / Casini, A. / Heine, A. / Kuhn, D. / Supuran, C.T. / Scozzafava, A. / Klebe, G. | ||||||
History |
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Remark 999 | SEQRES Residues 125 and 127 are adjacent in the sequence. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 128.1 KB | Display | ![]() |
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PDB format | ![]() | 97.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1cilS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29157.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: From human erythrocytes / Source: (natural) ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-CEL / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.73 Å3/Da / Density % sol: 28.8 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.2 Details: Tris-HCl, NaCl, ammonium sulfate, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 26, 2002 |
Radiation | Monochromator: Osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→30 Å / Num. all: 35103 / Num. obs: 35103 / % possible obs: 91.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rsym value: 0.093 / Net I/σ(I): 18.8 |
Reflection shell | Resolution: 1.5→1.53 Å / Mean I/σ(I) obs: 2.8 / Num. unique all: 694 / Rsym value: 0.311 / % possible all: 37 |
Reflection | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 30 Å / Num. measured all: 123343 / Rmerge(I) obs: 0.093 |
Reflection shell | *PLUS Highest resolution: 1.5 Å / % possible obs: 37 % / Rmerge(I) obs: 0.311 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1CIL Resolution: 1.5→10 Å / Num. parameters: 20762 / Num. restraintsaints: 26228 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: ANISOTROPIC SCALING APPLIED BY THE METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56 ANISOTROPIC REFINEMENT
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Displacement parameters | Biso mean: 22.3 Å2 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 2 / Occupancy sum hydrogen: 1983 / Occupancy sum non hydrogen: 2296 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 10 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.184 / Rfactor Rwork: 0.127 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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