+Open data
-Basic information
Entry | Database: PDB / ID: 1p8j | |||||||||
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Title | CRYSTAL STRUCTURE OF THE PROPROTEIN CONVERTASE FURIN | |||||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / PROHORMONE CONVERTASE / SPC1 / PACE / P-DOMAIN / CHLOROMETHYLKETONE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | Function and homology information : / zymogen inhibition / Assembly of active LPL and LIPC lipase complexes / Formation of the cornified envelope / Elastic fibre formation / trans-Golgi network transport vesicle membrane / NGF processing / Signaling by PDGF / Activation of Matrix Metalloproteinases / Removal of aminoterminal propeptides from gamma-carboxylated proteins ...: / zymogen inhibition / Assembly of active LPL and LIPC lipase complexes / Formation of the cornified envelope / Elastic fibre formation / trans-Golgi network transport vesicle membrane / NGF processing / Signaling by PDGF / Activation of Matrix Metalloproteinases / Removal of aminoterminal propeptides from gamma-carboxylated proteins / : / Pre-NOTCH Processing in Golgi / TGF-beta receptor signaling activates SMADs / Collagen degradation / : / furin / nerve growth factor production / dibasic protein processing / peptide biosynthetic process / Golgi cisterna / negative regulation of transforming growth factor beta1 production / signal peptide processing / negative regulation of low-density lipoprotein particle receptor catabolic process / secretion by cell / nerve growth factor binding / trans-Golgi network transport vesicle / blastocyst formation / zymogen activation / regulation of endopeptidase activity / peptide hormone processing / regulation of protein catabolic process / positive regulation of transforming growth factor beta receptor signaling pathway / regulation of signal transduction / viral life cycle / peptide binding / trans-Golgi network / serine-type endopeptidase inhibitor activity / protein processing / peptidase activity / endopeptidase activity / protease binding / membrane => GO:0016020 / early endosome / endosome membrane / positive regulation of cell migration / membrane raft / endoplasmic reticulum lumen / Golgi membrane / serine-type endopeptidase activity / endoplasmic reticulum membrane / cell surface / endoplasmic reticulum / extracellular region / membrane / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | |||||||||
Authors | Henrich, S. / Cameron, A. / Bourenkov, G.P. / Kiefersauer, R. / Huber, R. / Lindberg, I. / Bode, W. / Than, M.E. | |||||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2003 Title: The Crystal Structure of the Proprotein Processing Proteinase Furin Explains its Stringent Specificity Authors: Henrich, S. / Cameron, A. / Bourenkov, G.P. / Kiefersauer, R. / Huber, R. / Lindberg, I. / Bode, W. / Than, M.E. | |||||||||
History |
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Remark 650 | HELIX HELIX RECORDS IN THIS FILE WERE PROVIDED BY THE AUTHOR | |||||||||
Remark 700 | SHEET SHEET RECORDS IN THIS FILE WERE PROVIDED BY THE AUTHOR |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p8j.cif.gz | 763.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p8j.ent.gz | 638.5 KB | Display | PDB format |
PDBx/mmJSON format | 1p8j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p8/1p8j ftp://data.pdbj.org/pub/pdb/validation_reports/p8/1p8j | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
-Components
-Protein / Protein/peptide , 2 types, 16 molecules ABCDEFGHJKLMNPQR
#1: Protein | Mass: 51151.336 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: FURIN OR FUR OR PCSK3 / Plasmid: pcDNA3.1(-)-Myc-His / Organ (production host): Ovary cells / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): DG44 / References: UniProt: P23188, furin #2: Protein/peptide | |
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-Sugars , 3 types, 8 molecules
#3: Polysaccharide | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-[beta-D-galactopyranose- ...beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#4: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#5: Sugar | ChemComp-NAG / |
-Non-polymers , 3 types, 2391 molecules
#6: Chemical | ChemComp-CA / #7: Chemical | ChemComp-SO4 / #8: Water | ChemComp-HOH / | |
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-Details
Compound details | THE UNBOUND FORM OF THE INHIBITOR IS DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE. UPON REACTION ...THE UNBOUND FORM OF THE INHIBITOR IS DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETH |
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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: 3.78 Å3/Da / Density % sol: 67.46 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 1.0M (NH4)2SO4, 0.4M Li2SO4, 0.1M Na3Citrate, pH 6.0, VAPOR DIFFUSION, SITTING 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: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.05 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 28, 2001 / Details: mirrors |
Radiation | Monochromator: Si(111) double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.05 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→18.83 Å / Num. all: 182735 / Num. obs: 182735 / % possible obs: 97.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 27.4 Å2 / Rsym value: 0.1 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 2.6→2.74 Å / Rsym value: 0.347 / % possible all: 97.2 |
Reflection | *PLUS Num. measured all: 382735 / Rmerge(I) obs: 0.1 |
Reflection shell | *PLUS % possible obs: 97.2 % / Rmerge(I) obs: 0.347 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.6→18.82 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 1894579.24 / Data cutoff high rms absF: 1894579.24 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: waters 1-8: potential third calcium binding-site (identical to the suggest Ca401 binding site in subtilisin Carlsberg, 1CSE) waters 9-14: potential ion binding-site with low B factors
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 31.8965 Å2 / ksol: 0.326073 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→18.82 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.01 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Lowest resolution: 18.83 Å | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.31 |