[English] 日本語
![](img/lk-miru.gif)
- PDB-1fqm: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I/F95M/W97V CARBONIC ANH... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1fqm | ||||||
---|---|---|---|---|---|---|---|
Title | X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT | ||||||
![]() | CARBONIC ANHYDRASE | ||||||
![]() | LYASE / carbonic anhydrase / metal binding / metal specificity | ||||||
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 | ![]() | ||||||
![]() | Cox, J.D. / Hunt, J.A. / Compher, K.M. / Fierke, C.A. / Christianson, D.W. | ||||||
![]() | ![]() Title: Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II. Authors: Cox, J.D. / Hunt, J.A. / Compher, K.M. / Fierke, C.A. / Christianson, D.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 65.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 47 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 370 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 372.1 KB | Display | |
Data in XML | ![]() | 6.9 KB | Display | |
Data in CIF | ![]() | 10.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fqlC ![]() 1fqnC ![]() 1fqrC ![]() 1fr4C ![]() 1fr7C ![]() 1fsnC ![]() 1fsqC ![]() 1fsrC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is a monomer |
-
Components
#1: Protein | Mass: 29151.984 Da / Num. of mol.: 1 / Mutation: F93I/F95M/W97V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-HG / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.84 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: ammonium sulfate, tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 130 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Sep 8, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. all: 16456 / Num. obs: 15386 / % possible obs: 93.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 2.7 % / Biso Wilson estimate: 20.2 Å2 / Rmerge(I) obs: 0.059 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.121 / % possible all: 84.5 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / Num. measured all: 41762 |
Reflection shell | *PLUS % possible obs: 84.5 % |
-
Processing
Software |
| |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→20 Å
| |||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||
Software | *PLUS Name: ![]() | |||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / σ(F): 2 / % reflection Rfree: 5 % | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
|