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- PDB-1ugf: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ugf | ||||||
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Title | HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T) | ||||||
![]() | CARBONIC ANHYDRASE II | ||||||
![]() | LYASE / ACETYLATION / ZINC / POLYMORPHISM / DISEASE MUTATION | ||||||
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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Scolnick, L.R. / Christianson, D.W. | ||||||
![]() | ![]() Title: X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis. Authors: Scolnick, L.R. / Christianson, D.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 67 KB | Display | ![]() |
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PDB format | ![]() | 48 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368 KB | Display | ![]() |
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Full document | ![]() | 369.3 KB | Display | |
Data in XML | ![]() | 6.7 KB | Display | |
Data in CIF | ![]() | 10 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ugaC ![]() 1ugbC ![]() 1ugcC ![]() 1ugdC ![]() 1ugeC ![]() 1uggC C: citing same article ( |
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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: 29100.812 Da / Num. of mol.: 1 / Mutation: A65T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-HG / |
#3: Chemical | ChemComp-ZN / |
#4: Chemical | ChemComp-AZI / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||
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Crystal grow | pH: 8 / Details: 50MM TRIS-HCL, PH=8.0, 1.95 - 3.9M NH4SO4 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jan 15, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→7.2 Å / Num. obs: 17315 / % possible obs: 94.7 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Biso Wilson estimate: 16.2 Å2 / Rsym value: 0.059 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 2.4 % / Mean I/σ(I) obs: 3.2 / Rsym value: 0.16 / % possible all: 74.6 |
Reflection | *PLUS Num. measured all: 41320 / Rmerge(I) obs: 0.059 |
Reflection shell | *PLUS % possible obs: 74.6 % / Rmerge(I) obs: 0.16 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: NATIVE CAII, (HAKANSSON, ET AL., 1992) Resolution: 2→6.5 Å / Cross valid method: R-FREE / σ(F): 2
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Displacement parameters | Biso mean: 17.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 12 Å / Luzzati sigma a obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.24 |