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Yorodumi- PDB-1pwu: Crystal Structure of Anthrax Lethal Factor complexed with (3-(N-h... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1pwu | ||||||
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Title | Crystal Structure of Anthrax Lethal Factor complexed with (3-(N-hydroxycarboxamido)-2-isobutylpropanoyl-Trp-methylamide), a known small molecule inhibitor of matrix metalloproteases. | ||||||
Components | Lethal factor | ||||||
Keywords | HYDROLASE / Anthrax Toxin / Lethal Factor / small molecule peptidic inhibitor / hydroxamic acid. | ||||||
Function / homology | Function and homology information anthrax lethal factor endopeptidase / host cell cytosol / Uptake and function of anthrax toxins / metalloendopeptidase activity / metallopeptidase activity / toxin activity / proteolysis / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Bacillus anthracis (anthrax bacterium) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Wong, T.Y. / Schwarzenbacher, R. / Liddington, R.C. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2004 Title: The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor. Authors: Turk, B.E. / Wong, T.Y. / Schwarzenbacher, R. / Jarrell, E.T. / Leppla, S.H. / Collier, R.J. / Liddington, R.C. / Cantley, L.C. | ||||||
History |
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Remark 600 | heterogen GM6001 is a commercially available known inhibitor of matrix metalloproteases. It has an ...heterogen GM6001 is a commercially available known inhibitor of matrix metalloproteases. It has an N-terminal hydroxamic acid moeity with a Leu mimetic, followed by a Trp residue and a C-terminal methylamide. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pwu.cif.gz | 307.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pwu.ent.gz | 249.6 KB | Display | PDB format |
PDBx/mmJSON format | 1pwu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1pwu_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 1pwu_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 1pwu_validation.xml.gz | 56.9 KB | Display | |
Data in CIF | 1pwu_validation.cif.gz | 76.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pw/1pwu ftp://data.pdbj.org/pub/pdb/validation_reports/pw/1pwu | HTTPS FTP |
-Related structure data
Related structure data | 1pwqC 1pwvC 1pwwC 1j7nS 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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Details | The biological unit is a monomer. |
-Components
#1: Protein | Mass: 90330.836 Da / Num. of mol.: 2 / Mutation: E720C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus anthracis (anthrax bacterium) / Gene: LEF OR PXO1-107 / Plasmid: pX01 / Production host: Bacillus anthracis (anthrax bacterium) / Strain (production host): BH441 References: UniProt: P15917, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases #2: Chemical | #3: Chemical | |
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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: 3.6 Å3/Da / Density % sol: 65.5 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: Ammonium sulfate, Tris-HCl, EDTA., pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21-29 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 0.97 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 24, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. all: 72275 / Num. obs: 72275 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Rsym value: 0.083 / Net I/σ(I): 15.6 |
Reflection shell | Highest resolution: 2.7 Å / Mean I/σ(I) obs: 2.3 / % possible all: 98.8 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 50 Å / Num. measured all: 255861 / Rmerge(I) obs: 0.083 |
Reflection shell | *PLUS % possible obs: 98.8 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 2.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ID 1J7N Resolution: 2.7→33.1 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 256376.7 / Data cutoff high rms absF: 256376.7 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 37.8433 Å2 / ksol: 0.341304 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 61.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→33.1 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.87 Å / Rfactor Rfree error: 0.018 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Lowest resolution: 50 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.268 / Rfactor Rwork: 0.23 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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