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Yorodumi- PDB-1ezm: THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ezm | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION | ||||||
Components | PSEUDOMONAS ELASTASE | ||||||
Keywords | HYDROLASE | ||||||
Function / homology | Function and homology information pseudolysin / protein transport by the Sec complex / protein secretion by the type II secretion system / bacterial-type flagellum-dependent swarming motility / single-species biofilm formation / metalloendopeptidase activity / endopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.5 Å | ||||||
Authors | Thayer, M.M. / Flaherty, K.M. / Mckay, D.B. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1991 Title: Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. Authors: Thayer, M.M. / Flaherty, K.M. / McKay, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ezm.cif.gz | 72.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ezm.ent.gz | 53.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ezm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ezm_validation.pdf.gz | 364.8 KB | Display | wwPDB validaton report |
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Full document | 1ezm_full_validation.pdf.gz | 370.1 KB | Display | |
Data in XML | 1ezm_validation.xml.gz | 7.6 KB | Display | |
Data in CIF | 1ezm_validation.cif.gz | 11.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ez/1ezm ftp://data.pdbj.org/pub/pdb/validation_reports/ez/1ezm | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE 59 IS A CIS PROLINE. 2: THE PEPTIDE BOND BETWEEN RESIDUES TYR 63 AND LYS 64 IS IN CIS CONFORMATION. |
-Components
#1: Protein | Mass: 33175.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / References: UniProt: P14756, pseudolysin |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 42.01 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS 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: 1.42 Å / Lowest resolution: 30 Å / % possible obs: 69 % / Observed criterion σ(I): 2 / Num. measured all: 34624 / Rmerge(I) obs: 0.067 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.176 / Rfactor obs: 0.176 / Highest resolution: 1.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.5 Å / Num. reflection obs: 34276 / Rfactor obs: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.7 |