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Yorodumi- PDB-1arc: THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1arc | ||||||
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Title | THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE | ||||||
Components | ACHROMOBACTER PROTEASE I | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information lysyl endopeptidase / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | Achromobacter lyticus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Kitagawa, Y. / Katsube, Y. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1989 Title: The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease. Authors: Tsunasawa, S. / Masaki, T. / Hirose, M. / Soejima, M. / Sakiyama, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1arc.cif.gz | 61.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1arc.ent.gz | 44.1 KB | Display | PDB format |
PDBx/mmJSON format | 1arc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1arc_validation.pdf.gz | 436.4 KB | Display | wwPDB validaton report |
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Full document | 1arc_full_validation.pdf.gz | 439.9 KB | Display | |
Data in XML | 1arc_validation.xml.gz | 7.2 KB | Display | |
Data in CIF | 1arc_validation.cif.gz | 10.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ar/1arc ftp://data.pdbj.org/pub/pdb/validation_reports/ar/1arc | 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: 27759.227 Da / Num. of mol.: 1 / Fragment: residues 206-473 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Achromobacter lyticus (bacteria) / References: UniProt: P15636, lysyl endopeptidase |
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#2: Chemical | ChemComp-TCK / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.75 % |
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Crystal grow | *PLUS Method: other |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.152 / Highest resolution: 2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Rfactor obs: 0.152 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |