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Yorodumi- PDB-5om6: Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo2:... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5om6 | ||||||
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Title | Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo2: a MMP9-cleavable drug-binding serpin for doxycycline | ||||||
Components | (Alpha-1-antichymotrypsin) x 2 | ||||||
Keywords | TRANSPORT PROTEIN / Serpin / alpha1-Antichymotrypsin / Doxycycline-binding protein / MMP9-cleavable RCL | ||||||
Function / homology | Function and homology information maintenance of gastrointestinal epithelium / regulation of lipid metabolic process / platelet alpha granule lumen / acute-phase response / serine-type endopeptidase inhibitor activity / azurophil granule lumen / Platelet degranulation / secretory granule lumen / collagen-containing extracellular matrix / blood microparticle ...maintenance of gastrointestinal epithelium / regulation of lipid metabolic process / platelet alpha granule lumen / acute-phase response / serine-type endopeptidase inhibitor activity / azurophil granule lumen / Platelet degranulation / secretory granule lumen / collagen-containing extracellular matrix / blood microparticle / inflammatory response / Neutrophil degranulation / DNA binding / extracellular space / extracellular exosome / extracellular region / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.849 Å | ||||||
Authors | Schmidt, K. / Muller, Y.A. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018 Title: Design of an allosterically modulated doxycycline and doxorubicin drug-binding protein. Authors: Schmidt, K. / Gardill, B.R. / Kern, A. / Kirchweger, P. / Borsch, M. / Muller, Y.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5om6.cif.gz | 172.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5om6.ent.gz | 135 KB | Display | PDB format |
PDBx/mmJSON format | 5om6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5om6_validation.pdf.gz | 484.4 KB | Display | wwPDB validaton report |
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Full document | 5om6_full_validation.pdf.gz | 487.6 KB | Display | |
Data in XML | 5om6_validation.xml.gz | 31.8 KB | Display | |
Data in CIF | 5om6_validation.cif.gz | 45.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/om/5om6 ftp://data.pdbj.org/pub/pdb/validation_reports/om/5om6 | HTTPS FTP |
-Related structure data
Related structure data | 5om2C 5om3C 5om5C 5om7C 5om8C 6ftpC 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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2 |
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Unit cell |
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-Components
-Protein / Protein/peptide , 2 types, 4 molecules ACBD
#1: Protein | Mass: 41924.457 Da / Num. of mol.: 2 / Fragment: UNP residues 36-383 Mutation: L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q Source method: isolated from a genetically manipulated source Details: N-terminal residues that are present in the sample sequence but not in the PDB file could not be modelled due to missing electron density. C-terminal residues (ITA...KQA) are in chain I and K Source: (gene. exp.) Homo sapiens (human) / Gene: SERPINA3, AACT, GIG24, GIG25 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Star / References: UniProt: P01011 #2: Protein/peptide | Mass: 4762.639 Da / Num. of mol.: 2 / Fragment: UNP residues 384-423 Mutation: L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SERPINA3, AACT, GIG24, GIG25 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Star / References: UniProt: P01011 |
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-Non-polymers , 4 types, 379 molecules
#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-CL / | #6: 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: 2.32 Å3/Da / Density % sol: 46.9 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M citric acid pH 3.5, 25 % w/v PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Sep 15, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 1.849→38.601 Å / Num. obs: 72070 / % possible obs: 98.7 % / Redundancy: 3.8 % / Biso Wilson estimate: 33.2 Å2 / CC1/2: 0.999 / Rrim(I) all: 0.068 / Net I/σ(I): 15.2 |
Reflection shell | Resolution: 1.85→1.96 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 2.1 / Num. unique obs: 11566 / CC1/2: 0.766 / Rrim(I) all: 0.748 / % possible all: 98.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.849→38.601 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 27.61
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.849→38.601 Å
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Refine LS restraints |
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LS refinement shell |
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