+Open data
-Basic information
Entry | Database: PDB / ID: 1and | ||||||
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Title | ANIONIC TRYPSIN MUTANT WITH ARG 96 REPLACED BY HIS | ||||||
Components | ANIONIC TRYPSIN | ||||||
Keywords | SERINE PROTEASE / TRYPSIN / ANIONIC / HYDROLASE | ||||||
Function / homology | Function and homology information Antimicrobial peptides / Alpha-defensins / Activation of Matrix Metalloproteinases / trypsin / Neutrophil degranulation / digestion / collagen catabolic process / response to nutrient / serine-type endopeptidase activity / calcium ion binding ...Antimicrobial peptides / Alpha-defensins / Activation of Matrix Metalloproteinases / trypsin / Neutrophil degranulation / digestion / collagen catabolic process / response to nutrient / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Rattus rattus (black rat) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Fletterick, R.J. / Mcgrath, M.E. | ||||||
Citation | Journal: Biochemistry / Year: 1993 Title: Structure of an engineered, metal-actuated switch in trypsin. Authors: McGrath, M.E. / Haymore, B.L. / Summers, N.L. / Craik, C.S. / Fletterick, R.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1and.cif.gz | 54.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1and.ent.gz | 41.6 KB | Display | PDB format |
PDBx/mmJSON format | 1and.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1and_validation.pdf.gz | 378.1 KB | Display | wwPDB validaton report |
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Full document | 1and_full_validation.pdf.gz | 381.3 KB | Display | |
Data in XML | 1and_validation.xml.gz | 6.6 KB | Display | |
Data in CIF | 1and_validation.cif.gz | 10 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/1and ftp://data.pdbj.org/pub/pdb/validation_reports/an/1and | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 23795.791 Da / Num. of mol.: 1 / Mutation: R96H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus rattus (black rat) / Production host: Escherichia coli (E. coli) / References: UniProt: P00763, trypsin |
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#2: Chemical | ChemComp-CU / |
#3: Chemical | ChemComp-BEN / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.34 Å3/Da / Density % sol: 63 % | ||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | ||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1992 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.3 Å / Num. obs: 13200 / Redundancy: 2 % / Rsym value: 0.07 |
Reflection | *PLUS Num. measured all: 26500 / Rmerge(I) obs: 0.07 |
-Processing
Software |
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Refinement | Resolution: 2.3→7 Å / Rfactor Rwork: 0.161 / Rfactor obs: 0.161 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |