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Yorodumi- PDB-1mu0: Crystal Structure of the Tricorn Interacting Factor F1 Complex wi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mu0 | ||||||
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Title | Crystal Structure of the Tricorn Interacting Factor F1 Complex with PCK | ||||||
Components | Proline iminopeptidase | ||||||
Keywords | HYDROLASE / ALPHA-BETA HYDROLASE / CAP DOMAIN / CAGED ACTIVE SITE / PROLYL PEPTIDASE | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thermoplasma acidophilum (acidophilic) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Goettig, P. / Groll, M. / Kim, J.-S. / Huber, R. / Brandstetter, H. | ||||||
Citation | Journal: Embo J. / Year: 2002 Title: Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism Authors: Goettig, P. / Groll, M. / Kim, J.-S. / Huber, R. / Brandstetter, H. | ||||||
History |
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Remark 600 | HETEROGEN THE REACTION OF PHENYLALANYLCHLOROMETHYL KETONE (PCK) WITH SER105 RESULTED IN A ... HETEROGEN THE REACTION OF PHENYLALANYLCHLOROMETHYL KETONE (PCK) WITH SER105 RESULTED IN A COVALENTLY BOUND HETEROMOLECULE (PHK). |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mu0.cif.gz | 66.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mu0.ent.gz | 53.3 KB | Display | PDB format |
PDBx/mmJSON format | 1mu0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mu0_validation.pdf.gz | 429 KB | Display | wwPDB validaton report |
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Full document | 1mu0_full_validation.pdf.gz | 435.8 KB | Display | |
Data in XML | 1mu0_validation.xml.gz | 13.6 KB | Display | |
Data in CIF | 1mu0_validation.cif.gz | 17.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/1mu0 ftp://data.pdbj.org/pub/pdb/validation_reports/mu/1mu0 | HTTPS FTP |
-Related structure data
Related structure data | 1mt3SC 1mtzC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is the monomer in the asymmetric unit |
-Components
#1: Protein | Mass: 33530.090 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermoplasma acidophilum (acidophilic) / Gene: TA0830 / Plasmid: pRset6c / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: P96084, prolyl aminopeptidase |
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#2: Chemical | ChemComp-PHK / ( |
#3: 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: 2.13 Å3/Da / Density % sol: 42.27 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 12% PEG 6000, 100 mM Bis-Tris-HCl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 10, 2002 / Details: Osmic mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. all: 12507 / Num. obs: 12507 / % possible obs: 85.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 / Biso Wilson estimate: 22.1 Å2 / Net I/σ(I): 3.2 |
Reflection | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 20 Å / Num. obs: 11344 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1MT3 Resolution: 2.4→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 23.5 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 9958 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 0.948 |