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Yorodumi- PDB-1smp: CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1smp | ||||||
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Title | CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALLO-PROTEASE AND AN INHIBITOR FROM ERWINIA CHRYSANTHEMI | ||||||
Components |
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Keywords | COMPLEX (METALLOPROTEASE/INHIBITOR) / COMPLEX (METALLOPROTEASE-INHIBITOR) / COMPLEX (METALLOPROTEASE-INHIBITOR) complex | ||||||
Function / homology | Function and homology information serralysin / symbiont-mediated killing of host cell / metalloendopeptidase inhibitor activity / extracellular matrix / metalloendopeptidase activity / toxin activity / periplasmic space / calcium ion binding / proteolysis / extracellular space ...serralysin / symbiont-mediated killing of host cell / metalloendopeptidase inhibitor activity / extracellular matrix / metalloendopeptidase activity / toxin activity / periplasmic space / calcium ion binding / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Serratia marcescens (bacteria) Erwinia chrysanthemi (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Baumann, U. / Bauer, M. / Letoffe, S. / Delepelaire, P. / Wandersman, C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. Authors: Baumann, U. / Bauer, M. / Letoffe, S. / Delepelaire, P. / Wandersman, C. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Crystal Structure of the 50 kDa Metallo-Proteinase from Serratia Marcescens Authors: Baumann, U. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1smp.cif.gz | 122 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1smp.ent.gz | 98.9 KB | Display | PDB format |
PDBx/mmJSON format | 1smp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sm/1smp ftp://data.pdbj.org/pub/pdb/validation_reports/sm/1smp | HTTPS FTP |
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-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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-Components
#1: Protein | Mass: 50439.195 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Serratia marcescens (bacteria) / Gene: INH / Plasmid: PUC / Gene (production host): INH / Production host: Escherichia coli (E. coli) / References: UniProt: P23694, serralysin | ||
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#2: Protein | Mass: 11020.430 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Erwinia chrysanthemi (bacteria) / Genus: Dickeya / Gene: INH / Plasmid: PUC / Gene (production host): INH / Production host: Escherichia coli (E. coli) / References: UniProt: P18958 | ||
#3: Chemical | ChemComp-ZN / | ||
#4: Chemical | ChemComp-CA / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.24 Å3/Da / Density % sol: 70.96 % | |||||||||||||||
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Crystal | *PLUS Density % sol: 70 % | |||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 9 / PH range high: 8 | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS X1000 / Detector: AREA DETECTOR / Date: Mar 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 40845 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.057 |
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 54249 / Num. measured all: 192406 / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.35 Å / % possible obs: 76 % / Rmerge(I) obs: 0.211 |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 30.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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