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Yorodumi- PDB-1e1h: Crystal Structure of recombinant Botulinum Neurotoxin Type A Ligh... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1e1h | ||||||
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Title | Crystal Structure of recombinant Botulinum Neurotoxin Type A Light Chain, self-inhibiting Zn endopeptidase. | ||||||
Components | (BOTULINUM NEUROTOXIN TYPE A LIGHT CHAIN) x 2 | ||||||
Keywords | HYDROLASE / NEUROTOXIN / ZN-ENDOPEPTIDASE / COMPLEX / SUBSTRATE BOUND / BOTULINUM / INHIBITOR BOUND | ||||||
Function / homology | Function and homology information bontoxilysin / host cell presynaptic membrane / host cell cytoplasmic vesicle / host cell cytosol / protein transmembrane transporter activity / metalloendopeptidase activity / toxin activity / host cell plasma membrane / proteolysis / zinc ion binding ...bontoxilysin / host cell presynaptic membrane / host cell cytoplasmic vesicle / host cell cytosol / protein transmembrane transporter activity / metalloendopeptidase activity / toxin activity / host cell plasma membrane / proteolysis / zinc ion binding / extracellular region / membrane Similarity search - Function | ||||||
Biological species | CLOSTRIDIUM BOTULINUM (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Knapp, M. / Rupp, B. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Crystal Structure of Clostridium Botulinum Neurotoxin Protease in a Product-Bound State: Evidence for Noncanonical Zinc Protease Activity Authors: Segelke, B.W. / Knapp, M. / Kadhkodayan, S. / Balhorn, R. / Rupp, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e1h.cif.gz | 190.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e1h.ent.gz | 148.8 KB | Display | PDB format |
PDBx/mmJSON format | 1e1h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e1/1e1h ftp://data.pdbj.org/pub/pdb/validation_reports/e1/1e1h | HTTPS FTP |
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-Related structure data
Related structure data | 3btaS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 32153.004 Da / Num. of mol.: 2 / Fragment: RESIDUES 10-250 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CLOSTRIDIUM BOTULINUM (bacteria) / Strain: KYOTO-F / Production host: ESCHERICHIA COLI (E. coli) / Variant (production host): BLR DE-3 / References: UniProt: Q45894, bontoxilysin #2: Protein | Mass: 20560.143 Da / Num. of mol.: 2 / Fragment: RESIDUES 252-416 / Mutation: YES Source method: isolated from a genetically manipulated source Details: HOMODIMER, CONTAINING CLEAVED SUBSTRATE ANALOG (LOOP 245-255) IN ACTIVE SITE Source: (gene. exp.) CLOSTRIDIUM BOTULINUM (bacteria) / Strain: KYOTO-F / Production host: ESCHERICHIA COLI (E. coli) / Variant (production host): BLR DE-3 / References: UniProt: Q45894, bontoxilysin #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | TER TYR: PEPTIDE CHAIN CLEAVED AT AA 249 AND 250. HIS: PEPTIDE CHAIN CLEAVED AT AA 249 AND 250. | Sequence details | EXPERIMENTAL PROTEIN HAS 6XHIS-TAG AND S-TAG AT N-TERMINUS FOLLOWED BY RESIDUES 9-415 OF NCBI: ...EXPERIMENT | |
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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: 2.91 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 4.6 Details: HANGING DROP VAPOUR DIFFUSION, DROP: 4UL 5MG/ML PROTEIN & 2UL WELL. PROTEIN: 0.05M TRIS PH 8.0,10% GLYCEROL, 0.1% TRITON X-100,1.0MM 2-ME,4% XYLITOL. WELL: 0.2M (NH4)2SO4,0.1M NAOAC PH 4.6, 25% PEG4000. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 125 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1.1 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jan 15, 2000 / Details: DOUBLE FOCUSSING |
Radiation | Monochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→19.34 Å / Num. obs: 93168 / % possible obs: 95.2 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Biso Wilson estimate: 24.47 Å2 / Rsym value: 0.042 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 1.7 / Rsym value: 0.383 / % possible all: 95.2 |
Reflection | *PLUS Highest resolution: 1.8 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.042 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.9 Å / Redundancy: 1.9 % / Num. unique obs: 6918 / Rmerge(I) obs: 0.383 / Mean I/σ(I) obs: 1.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: LC COORDINATES OF PDB ENTRY 3BTA Resolution: 1.8→19.34 Å / SU B: 2.746 / SU ML: 0.085 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.129 / ESU R Free: 0.127
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Displacement parameters | Biso mean: 31.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→19.34 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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