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Yorodumi- PDB-2evo: crystal structure of methionine amino peptidase in complex with N... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2evo | ||||||
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Title | crystal structure of methionine amino peptidase in complex with N-cyclopentyl-N-(thiazol-2-yl)oxalamide | ||||||
Components | Methionine aminopeptidase | ||||||
Keywords | HYDROLASE / methionine aminopeptidase / complex | ||||||
Function / homology | Function and homology information initiator methionyl aminopeptidase activity / methionyl aminopeptidase / metalloaminopeptidase activity / ferrous iron binding / proteolysis / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Huang, W.-J. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2006 Title: Structural analysis of metalloform-selective inhibition of methionine aminopeptidase. Authors: Xie, S.X. / Huang, W.J. / Ma, Z.Q. / Huang, M. / Hanzlik, R.P. / Ye, Q.Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2evo.cif.gz | 119.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2evo.ent.gz | 91.3 KB | Display | PDB format |
PDBx/mmJSON format | 2evo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2evo_validation.pdf.gz | 456.1 KB | Display | wwPDB validaton report |
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Full document | 2evo_full_validation.pdf.gz | 461.5 KB | Display | |
Data in XML | 2evo_validation.xml.gz | 23.8 KB | Display | |
Data in CIF | 2evo_validation.cif.gz | 33.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ev/2evo ftp://data.pdbj.org/pub/pdb/validation_reports/ev/2evo | HTTPS FTP |
-Related structure data
Related structure data | 2evcC 2evmC 2matS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 29370.838 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: map / Plasmid: pGEMEX-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P0AE18, methionyl aminopeptidase #2: Chemical | ChemComp-CO / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 35.1 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion / pH: 7.5 Details: 15% PEG 8000, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 7, 2004 / Details: mirrors |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. all: 43944 / Num. obs: 48408 / % possible obs: 92.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.7→2.1 Å / % possible all: 89.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2mat Resolution: 1.7→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→20 Å
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Refine LS restraints |
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