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Yorodumi- PDB-1c5w: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING,... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1c5w | |||||||||
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Title | STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR | |||||||||
Components | (PROTEIN (UROKINASE-TYPE PLASMINOGEN ACTIVATOR)) x 2 | |||||||||
Keywords | BLOOD CLOTTING / selective / S1 site inhibitor / structure-based drug design / urokinase / trypsin / thrombin | |||||||||
Function / homology | Function and homology information u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / regulation of signaling receptor activity / negative regulation of plasminogen activation / regulation of smooth muscle cell migration ...u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / regulation of signaling receptor activity / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / serine-type endopeptidase complex / Dissolution of Fibrin Clot / smooth muscle cell migration / plasminogen activation / regulation of cell adhesion mediated by integrin / tertiary granule membrane / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / serine protease inhibitor complex / fibrinolysis / chemotaxis / blood coagulation / regulation of cell population proliferation / response to hypoxia / positive regulation of cell migration / external side of plasma membrane / 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 / DIFFERENCE FOURIER PLUS REFINEMENT / Resolution: 1.94 Å | |||||||||
Authors | Katz, B.A. / Mackman, R. / Luong, C. / Radika, K. / Martelli, A. / Sprengeler, P.A. / Wang, J. / Chan, H. / Wong, L. | |||||||||
Citation | Journal: Chem.Biol. / Year: 2000 Title: Structural basis for selectivity of a small molecule, S1-binding, submicromolar inhibitor of urokinase-type plasminogen activator. Authors: Katz, B.A. / Mackman, R. / Luong, C. / Radika, K. / Martelli, A. / Sprengeler, P.A. / Wang, J. / Chan, H. / Wong, L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c5w.cif.gz | 133.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c5w.ent.gz | 106.8 KB | Display | PDB format |
PDBx/mmJSON format | 1c5w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1c5w_validation.pdf.gz | 761.1 KB | Display | wwPDB validaton report |
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Full document | 1c5w_full_validation.pdf.gz | 769.6 KB | Display | |
Data in XML | 1c5w_validation.xml.gz | 17.4 KB | Display | |
Data in CIF | 1c5w_validation.cif.gz | 25.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c5/1c5w ftp://data.pdbj.org/pub/pdb/validation_reports/c5/1c5w | HTTPS FTP |
-Related structure data
Related structure data | 1c5lC 1c5mC 1c5nC 1c5oC 1c5pC 1c5qC 1c5rC 1c5sC 1c5tC 1c5uC 1c5vC 1c5xC 1c5yC 1c5zC 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein/peptide | Mass: 2708.183 Da / Num. of mol.: 1 / Fragment: SHORT CHAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PPIC9 / Production host: Pichia pastoris (fungus) / Strain (production host): HISTIDINE DEFICIENT GS115 / References: UniProt: P00749, u-plasminogen activator | ||||
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#2: Protein | Mass: 28435.428 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PPIC9 / Production host: Pichia pastoris (fungus) / Strain (production host): HISTIDINE DEFICIENT GS115 / References: UniProt: P00749, u-plasminogen activator | ||||
#3: Chemical | #4: Chemical | ChemComp-ESI / | #5: 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: 2 Å3/Da / Density % sol: 25.6 % |
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Crystal grow | pH: 6.5 Details: LMW human uPA/A145 was concentrated to 10 mg/ml and incubated in 50 mM HEPES, 5.0 mM NaCl. pH 7.0, 1.4 mM 4-iodobenzo[b]thiophene-2-carboxamidine for 15 min on ice. The complex was ...Details: LMW human uPA/A145 was concentrated to 10 mg/ml and incubated in 50 mM HEPES, 5.0 mM NaCl. pH 7.0, 1.4 mM 4-iodobenzo[b]thiophene-2-carboxamidine for 15 min on ice. The complex was crystallized by vapor diffusion in hanging drops containing equal volumes of protein-inhibitor solution (0.28 mM uPA/A145, 1.4 mM inhibitor) and well solution (20 % 2-propanol, 20 % PEG 4K, 100 mM sodium citrate, pH 6.5) sealed over the well. |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Mar 22, 1998 / Details: MSC MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→41.52 Å / Num. all: 15791 / % possible obs: 79 % / Observed criterion σ(I): 1 / Redundancy: 2.4 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 6.3 |
Reflection shell | Resolution: 1.94→2.03 Å / Rmerge(I) obs: 0.195 / Mean I/σ(I) obs: 2.3 / % possible all: 49.5 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER PLUS REFINEMENT Starting model: PDB1LMW Resolution: 1.94→7.5 Å / Cross valid method: X-PLOR / σ(F): 2 Details: Bulk solvent terms included in Fob file created with standard X-PLOR script. Only Leu A9 to Thr_A17 are included for the A-chain. Residues prior and after these residues are not visible ...Details: Bulk solvent terms included in Fob file created with standard X-PLOR script. Only Leu A9 to Thr_A17 are included for the A-chain. Residues prior and after these residues are not visible (disordered). Residues after Glu_B245 are not visible (disordered). Residues simultaneously refined in two or more conformations are: Ile_B17, Val_B38, Met_B47, Met_B81, Glu_B86, Leu_B123, Thr_B139, Arg_B166, Gln_B192, Lys_B223, Ser_B232 No energy terms between citrate 1 and 2 are included because they appear to be hydrogen-bonded to one another via an unusually short hydrogen bond between carboxylate groups. Disordered waters are: HOH33 which is close to HOH36; HOH303 which is close to HOH306; HOH715 which is close to HOH720; HOH945 which is close to a symmetry-related equivalent of itself; HOH946 which is close to a symmetry-related equivalent of itself; HOH838 which is close to HOH853.
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Refinement step | Cycle: LAST / Resolution: 1.94→7.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.03→1.94 Å / Total num. of bins used: 8
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Xplor file |
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