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- PDB-6m9d: PSEUDOMONAS SERINE-CARBOXYL PROTEINASE (SEDOLISIN) COMPLEXED WITH... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6m9d | ||||||||||||
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Title | PSEUDOMONAS SERINE-CARBOXYL PROTEINASE (SEDOLISIN) COMPLEXED WITH THE INHIBITOR Chymostatin | ||||||||||||
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![]() | Hydrolase/Hydrolase inhibitor / Serine-carboxyl proteinase / Hydrolase-hydrolase inhibitor complex | ||||||||||||
Function / homology | ![]() sedolisin / tripeptidyl-peptidase activity / periplasmic space / serine-type endopeptidase activity / proteolysis / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() synthetic construct (others) | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Wlodawer, A. / Li, M. / Gustchina, A. / Dauter, Z. / Uchida, K. / Oyama, H. / Goldfarb, N.E. / Dunn, B.M. / Oda, K. | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase Authors: Wlodawer, A. / Li, M. / Gustchina, A. / Dauter, Z. / Uchida, K. / Oyama, H. / Goldfarb, N.E. / Dunn, B.M. / Oda, K. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 143.3 KB | Display | ![]() |
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PDB format | ![]() | 110.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436 KB | Display | ![]() |
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Full document | ![]() | 438.3 KB | Display | |
Data in XML | ![]() | 17.5 KB | Display | |
Data in CIF | ![]() | 25.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6m8wC ![]() 6m8yC ![]() 6m9cC ![]() 6m9fC ![]() 1ga6S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Details | AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS A MONOMER |
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Components
#1: Protein | Mass: 38108.848 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: 101 / Gene: pcp / Production host: ![]() ![]() |
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#2: Protein/peptide | ![]() Details: The first residue (PHE) of the inhibitor chymostatin A was not visible in the electron density map and is not modeled in the structure Source: (synth.) synthetic construct (others) / References: Chymostatin A (bound form) |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Compound details | THE UNBOUND INHIBITOR (CHAIN B) IS Chymostatin A (PHE-CSI-LEU-PHA), WITH C-TERMINAL PHENYLALANINAL. ...THE UNBOUND INHIBITOR (CHAIN B) IS Chymostatin A (PHE-CSI-LEU-PHA), WITH C-TERMINAL PHENYLALAN |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.02 Å3/Da / Density % sol: 59.28 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: Ammonium sulfate, guanidinium hydrochloride, glycerol |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 11, 2001 / Details: Mirrors | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2→30 Å / Num. obs: 28260 / % possible obs: 92.4 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.073 / Χ2: 1.012 / Net I/av σ(I): 16.7 / Net I/σ(I): 8.3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GA6 Resolution: 2→30 Å / Num. parameters: 11771 / Num. restraintsaints: 11294 / Cross valid method: THROUGHOUT
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Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 2529 / Occupancy sum non hydrogen: 2722 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 2→30 Å
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Refine LS restraints |
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