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- PDB-2psg: REFINED STRUCTURE OF PORCINE PEPSINOGEN AT 1.8 ANGSTROMS RESOLUTION -
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Open data
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Basic information
Entry | Database: PDB / ID: 2psg | ||||||
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Title | REFINED STRUCTURE OF PORCINE PEPSINOGEN AT 1.8 ANGSTROMS RESOLUTION | ||||||
![]() | PEPSINOGEN | ||||||
![]() | HYDROLASE(ACID PROTEINASE ZYMOGEN) | ||||||
Function / homology | ![]() Surfactant metabolism / pepsin A / digestion / aspartic-type endopeptidase activity / proteolysis / extracellular exosome Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | James, M.N.G. / Sielecki, A.R. | ||||||
![]() | ![]() Title: Refined structure of porcine pepsinogen at 1.8 A resolution. Authors: Sielecki, A.R. / Fujinaga, M. / Read, R.J. / James, M.N. #1: ![]() Title: Molecular Structure of an Aspartic Proteinase Zymogen, Porcine Pepsinogen, at 1.8 Angstroms Resolution Authors: James, M.N.G. / Sielecki, A.R. #2: ![]() Title: Characterization of Phosphoserine of Pepsinogen Using 31P Nuclear Magnetic Resonance: Corroboration of X-Ray Crystallographic Results Authors: Williams, S.P. / Bridger, W.A. / James, M.N.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 88.1 KB | Display | ![]() |
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PDB format | ![]() | 65.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 371.4 KB | Display | ![]() |
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Full document | ![]() | 383.9 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 16.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: RESIDUE PRO 23 IS A CIS PROLINE. 2: RESIDUE SER 68 IS PHOSHORYLATED. THE PHOSPHATE GROUP IS PRESENTED AS HET GROUP PO3 ON HET RECORDS AT THE END OF THE CHAIN. | ||||||||
Components on special symmetry positions |
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Components
#1: Protein | Mass: 39631.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Sequence details | THE SEQUENCE USED IN THIS ENTRY IS THAT OF P.SEPULVEDA, J.MARCINISZYN JR.,D.LIU,J.TANG (J.BIO.CHEM. ...THE SEQUENCE USED IN THIS ENTRY IS THAT OF P.SEPULVEDA, J.MARCINISZY |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.05 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.1 / Method: vapor diffusion, hanging drop / Details: took James & Sielecki, 1986 from original paper | ||||||||||||||||||||||||
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: 40 Å / Num. obs: 27251 / Observed criterion σ(I): 2 / Num. measured all: 37575 / Rmerge(I) obs: 0.058 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→8 Å / σ(I): 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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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.164 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 15 Å2 |