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- PDB-1aks: CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORC... -
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Basic information
Entry | Database: PDB / ID: 1aks | ||||||
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Title | CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN | ||||||
![]() | (ALPHA TRYPSIN) x 2 | ||||||
![]() | SERINE PROTEASE / HYDROLASE | ||||||
Function / homology | ![]() trypsin / digestion / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Johnson, A. / Krishnaswamy, S. / Sundaram, P.V. / Pattabhi, V. | ||||||
![]() | ![]() Title: The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin. 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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PDBx/mmCIF format | ![]() | 67.2 KB | Display | ![]() |
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PDB format | ![]() | 50.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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: 13303.996 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 10205.522 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Sequence details | THE 223 AMINO ACIDS OF TRYPSIN ARE IDENTIFIED BY THE RESIDUE NUMBERS OF THE HOMOLOGOUS ...THE 223 AMINO ACIDS OF TRYPSIN ARE IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.23 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 293 K / pH: 6.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 8 Å / Num. obs: 17486 / % possible obs: 95 % / Num. measured all: 56502 / Rmerge(I) obs: 0.08 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 2 Å / % possible obs: 91.3 % / Num. unique obs: 4585 / Num. measured obs: 15077 / Rmerge(I) obs: 0.661 |
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Processing
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Refinement | Resolution: 1.8→8 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.2 / Rfactor Rfree: 0.285 / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 2 Å / Rfactor Rfree: 0.31 / Rfactor obs: 0.27 |