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Yorodumi- PDB-3pb1: Crystal Structure of a Michaelis Complex between Plasminogen Acti... -
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-Basic information
Entry | Database: PDB / ID: 3pb1 | ||||||
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Title | Crystal Structure of a Michaelis Complex between Plasminogen Activator Inhibitor-1 and Urokinase-type Plasminogen Activator | ||||||
Components |
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Keywords | hydrolase Inhibitor/Hydrolase / PAI-1 / uPA / Michaelis complex / Structural Genomics / Structure 2 Function Project / S2F / hydrolase Inhibitor-Hydrolase complex | ||||||
Function / homology | Function and homology information positive regulation of leukotriene production involved in inflammatory response / dentinogenesis / negative regulation of smooth muscle cell-matrix adhesion / negative regulation of smooth muscle cell migration / peptidase inhibitor complex / negative regulation of vascular wound healing / negative regulation of wound healing / positive regulation of odontoblast differentiation / negative regulation of cell adhesion mediated by integrin / u-plasminogen activator ...positive regulation of leukotriene production involved in inflammatory response / dentinogenesis / negative regulation of smooth muscle cell-matrix adhesion / negative regulation of smooth muscle cell migration / peptidase inhibitor complex / negative regulation of vascular wound healing / negative regulation of wound healing / positive regulation of odontoblast differentiation / negative regulation of cell adhesion mediated by integrin / u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / negative regulation of blood coagulation / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / negative regulation of endopeptidase activity / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity / serine-type endopeptidase complex / Dissolution of Fibrin Clot / positive regulation of monocyte chemotaxis / smooth muscle cell migration / plasminogen activation / tertiary granule membrane / regulation of cell adhesion mediated by integrin / replicative senescence / ECM proteoglycans / positive regulation of blood coagulation / negative regulation of fibrinolysis / specific granule membrane / negative regulation of endothelial cell apoptotic process / regulation of cell adhesion / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / serine protease inhibitor complex / fibrinolysis / negative regulation of cell migration / BMAL1:CLOCK,NPAS2 activates circadian gene expression / platelet alpha granule lumen / positive regulation of interleukin-8 production / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / serine-type endopeptidase inhibitor activity / positive regulation of inflammatory response / positive regulation of receptor-mediated endocytosis / positive regulation of angiogenesis / chemotaxis / blood coagulation / Platelet degranulation / regulation of cell population proliferation / collagen-containing extracellular matrix / angiogenesis / cellular response to lipopolysaccharide / protease binding / defense response to Gram-negative bacterium / response to hypoxia / positive regulation of cell migration / external side of plasma membrane / signaling receptor binding / serine-type endopeptidase activity / focal adhesion / Neutrophil degranulation / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Lin, Z. / Jiang, L. / Huang, M. / Structure 2 Function Project (S2F) | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: Structural basis for recognition of urokinase-type plasminogen activator by plasminogen activator inhibitor-1. Authors: Lin, Z. / Jiang, L. / Yuan, C. / Jensen, J.K. / Zhang, X. / Luo, Z. / Furie, B.C. / Furie, B. / Andreasen, P.A. / Huang, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3pb1.cif.gz | 142.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3pb1.ent.gz | 108.9 KB | Display | PDB format |
PDBx/mmJSON format | 3pb1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pb/3pb1 ftp://data.pdbj.org/pub/pdb/validation_reports/pb/3pb1 | HTTPS FTP |
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-Related structure data
Related structure data | 1dvmS 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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-Components
#1: Protein | Mass: 42795.066 Da / Num. of mol.: 1 / Mutation: N150H, K154T, Q319L, M354I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SERPINE1, PAI1, PLANH1 / Production host: Escherichia coli (E. coli) / References: UniProt: P05121 | ||
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#2: Protein | Mass: 28426.373 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 143-395 / Mutation: S195A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PLAU, RP11-417O11.1-002 / Production host: Pichia pastoris (fungus) References: UniProt: Q5SWW8, UniProt: P00749*PLUS, u-plasminogen activator | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.33 Å3/Da / Density % sol: 63.02 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 1.4M ammonium sulfate, 0.1M Tris-HCl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å |
Detector | Detector: DIFFRACTOMETER / Date: Jun 16, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→99 Å / Num. all: 81438 / Num. obs: 80462 / % possible obs: 99.9 % / Redundancy: 5.9 % / Rmerge(I) obs: 0.162 / Rsym value: 0.185 / Net I/σ(I): 21.5 |
Reflection shell | Resolution: 2.3→2.34 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.589 / Mean I/σ(I) obs: 3.4 / Num. unique all: 3996 / Rsym value: 0.633 / % possible all: 98.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1DVM Resolution: 2.3→38.32 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.891 / SU B: 6.525 / SU ML: 0.16 / Cross valid method: THROUGHOUT / ESU R Free: 0.23 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.466 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→38.32 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.301→2.361 Å / Total num. of bins used: 20
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