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Open data
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Basic information
Entry | Database: PDB / ID: 1qqu | ||||||
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Title | CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH BOUND ACETATE ION | ||||||
![]() | BETA TRYPSIN | ||||||
![]() | HYDROLASE / SERINE PROTEASE | ||||||
Function / homology | ![]() trypsin / digestion / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Johnson, A. / Gautham, N. / Pattabhi, V. | ||||||
![]() | ![]() Title: Crystal structure at 1.63 A resolution of the native form of porcine beta-trypsin: revealing an acetate ion binding site and functional water network. Authors: Johnson, A. / Gautham, N. / Pattabhi, V. #1: ![]() Title: The First Crystal Structure at 1.8 Angstroms Resolution of an Active Autolysate Form of Porcine Alpha Trypsin Authors: Johnson, A. / Krishnaswamy, S. / Sundaram, P.V. / Pattabhi, V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 58.6 KB | Display | ![]() |
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PDB format | ![]() | 41.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1aksS 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: 23491.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-ACT / |
#4: Water | ChemComp-HOH / |
Sequence details | THE 223 AMINO ACIDS OF TRYPSIN ARE IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.81 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.7 / Details: pH 6.70 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: drop consists of equal volume of protein and precipitant solutions | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.54 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 13, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.63→23.62 Å / Num. obs: 21149 / % possible obs: 83.2 % / Observed criterion σ(I): 0 / Redundancy: 3.83 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 19.96 |
Reflection shell | Resolution: 1.63→1.7 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 2.77 / % possible all: 80.6 |
Reflection shell | *PLUS % possible obs: 80.6 % |
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Processing
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Refinement | Method to determine structure: MOLECULAR REPLCEMENT Starting model: 1AKS Resolution: 1.63→8 Å / Cross valid method: FREE R / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.63→8 Å
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Software | *PLUS Name: 'X-PLOR,REFMAC,CNS 0.9' / Classification: refinement | ||||||||||||||||||||
Refine LS restraints | *PLUS
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