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- PDB-2x95: Crystal structure of AnCE-lisinopril-tryptophan analogue, lisW-S ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2x95 | |||||||||
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Title | Crystal structure of AnCE-lisinopril-tryptophan analogue, lisW-S complex | |||||||||
![]() | ANGIOTENSIN CONVERTING ENZYME | |||||||||
![]() | HYDROLASE / METALLOPROTEASE / CARBOXYPEPTIDASE / ACE INHIBITOR / GLYCOPROTEIN | |||||||||
Function / homology | ![]() Metabolism of Angiotensinogen to Angiotensins / metamorphosis / response to symbiotic bacterium / peptidyl-dipeptidase A / sexual reproduction / positive regulation of systemic arterial blood pressure / peptide hormone processing / regulation of systemic arterial blood pressure by renin-angiotensin / peptidyl-dipeptidase activity / carboxypeptidase activity ...Metabolism of Angiotensinogen to Angiotensins / metamorphosis / response to symbiotic bacterium / peptidyl-dipeptidase A / sexual reproduction / positive regulation of systemic arterial blood pressure / peptide hormone processing / regulation of systemic arterial blood pressure by renin-angiotensin / peptidyl-dipeptidase activity / carboxypeptidase activity / metallopeptidase activity / proteolysis / extracellular space / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Akif, M. / Georgiadis, D. / Mahajan, A. / Dive, V. / Sturrock, E.D. / Isaac, R.E. / Acharya, K.R. | |||||||||
![]() | ![]() Title: High Resolution Crystal Structures of Drosophila Melanogaster Angiotensin Converting Enzyme in Complex with Novel Inhibitors and Anti- Hypertensive Drugs. Authors: Akif, M. / Georgiadis, D. / Mahajan, A. / Dive, V. / Sturrock, E.D. / Isaac, R.E. / Acharya, K.R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 146 KB | Display | ![]() |
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PDB format | ![]() | 116.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 29 KB | Display | |
Data in CIF | ![]() | 43.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2x8yC ![]() 2x8zC ![]() 2x90C ![]() 2x91C ![]() 2x92C ![]() 2x93C ![]() 2x94C ![]() 2x96C ![]() 2x97C 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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1 |
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 69239.680 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-615 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Sugars , 2 types, 3 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D- ...beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#5: Sugar |
-Non-polymers , 4 types, 520 molecules ![](data/chem/img/EPE.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/X95.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/X95.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | ChemComp-ZN / | #6: Chemical | ChemComp-X95 / ( | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.24 Å3/Da / Density % sol: 70.98 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jan 20, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→50 Å / Num. obs: 81744 / % possible obs: 87.2 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Biso Wilson estimate: 25.09 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 1.96→2.03 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 3.4 / % possible all: 87.5 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.503 Å2
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Refinement step | Cycle: LAST / Resolution: 1.96→32.63 Å
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Refine LS restraints |
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