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- PDB-4ufa: Crystal structure of the Angiotensin-1 converting enzyme N-domain... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4ufa | |||||||||
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Title | Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with Ac-SD | |||||||||
![]() | ANGIOTENSIN-CONVERTING ENZYME![]() | |||||||||
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Function / homology | ![]() mononuclear cell proliferation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Masuyer, G. / Douglas, R.G. / Sturrock, E.D. / Acharya, K.R. | |||||||||
![]() | ![]() Title: Structural Basis of Ac-Sdkp Hydrolysis by Angiotensin-I Converting Enzyme Authors: Masuyer, G. / Douglas, R.G. / Sturrock, E.D. / 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 | ![]() | 278.6 KB | Display | ![]() |
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PDB format | ![]() | 221.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4ufbC ![]() 3nxqS C: citing same article ( 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | ![]() Mass: 72606.508 Da / Num. of mol.: 2 / Fragment: N DOMAIN (UNP RESIDUES 30-657) / Mutation: YES Source method: isolated from a genetically manipulated source Details: MINIMALLY GLYCOSYLATED MUTANT / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: P12821, ![]() ![]() |
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-Sugars , 5 types, 6 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | 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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#3: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose![]() Source method: isolated from a genetically manipulated source |
#4: Polysaccharide | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose![]() Source method: isolated from a genetically manipulated source |
#5: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...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 |
#8: Sugar | ![]() |
-Non-polymers , 7 types, 791 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/P6G.gif)
![](data/chem/img/SAC.gif)
![](data/chem/img/ASP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/P6G.gif)
![](data/chem/img/SAC.gif)
![](data/chem/img/ASP.gif)
![](data/chem/img/HOH.gif)
#6: Chemical | #7: Chemical | ![]() #9: Chemical | ChemComp-PEG / ![]() #10: Chemical | ![]() #11: Chemical | #12: Chemical | ![]() #13: Water | ChemComp-HOH / | ![]() |
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-Details
Sequence details | P62328 RESIDUES 2-3 |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.8 % / Description: NONE |
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Crystal grow![]() | pH: 8.5 Details: 0.06 M DIVALENT CATIONS, 0.1 M TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 29, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.8→35.2 Å / Num. obs: 130327 / % possible obs: 90.4 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 6.1 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.65 / Mean I/σ(I) obs: 1.6 / % possible all: 57.6 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 3NXQ Resolution: 1.8→74.24 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.945 / SU B: 3.846 / SU ML: 0.112 / Cross valid method: THROUGHOUT / ESU R: 0.142 / ESU R Free: 0.129 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DI-PEPTIDE AC-SD IS PRODUCT OF AC-SDKP CLEAVAGE REACTION BY ACE
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.59 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→74.24 Å
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Refine LS restraints |
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