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- PDB-1c5q: STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING,... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c5q | ||||||
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Title | STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR | ||||||
![]() | PROTEIN (TRYPSIN) | ||||||
![]() | HYDROLASE / selective / S1 site inhibitor / structure-based drug design / urokinase / trypsin / thrombin | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Katz, B.A. / Mackman, R. / Luong, C. / Radika, K. / Martelli, A. / Sprengeler, P.A. / Wang, J. / Chan, H. / Wong, L. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.8 KB | Display | ![]() |
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PDB format | ![]() | 86.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 793 KB | Display | ![]() |
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Full document | ![]() | 793.7 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 20.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1c5lC ![]() 1c5mC ![]() 1c5nC ![]() 1c5oC ![]() 1c5pC ![]() 1c5rC ![]() 1c5sC ![]() 1c5tC ![]() 1c5uC ![]() 1c5vC ![]() 1c5wC ![]() 1c5xC ![]() 1c5yC ![]() 1c5zC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-CL / |
#4: Chemical | ChemComp-ESI / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.05 Å3/Da / Density % sol: 44.5 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.2 Details: trypsin-benzamidine, P2(1)2(1)2(1) were grown by vapor diffusion, as described for P2(1) 2(1) 2(1) (large cell) (Mangel, et al., Biochemistry 29, 8351-8357, 1990) The crystal was soaked in a ...Details: trypsin-benzamidine, P2(1)2(1)2(1) were grown by vapor diffusion, as described for P2(1) 2(1) 2(1) (large cell) (Mangel, et al., Biochemistry 29, 8351-8357, 1990) The crystal was soaked in a solution of 85 % MgSO4 . 7 H2O, 1 mM CaCl2, 2.0 % DMSO, saturated with inhibitor, 100 mM Tris, pH 8.20 over a period of several days with several replacements of the soaking solution. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: batch method / Details: Katz, B.A., (1999) J. Mol. Biol., 292, 669. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Oct 14, 1997 / 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: 1.33→31.93 Å / Num. all: 41527 / % possible obs: 75 % / Observed criterion σ(I): 1 / Redundancy: 2.1 % / Rmerge(I) obs: 0.087 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 1.43→1.49 Å / Rmerge(I) obs: 0.259 / Mean I/σ(I) obs: 2.1 / % possible all: 39.1 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER PLUS REFINEMENT Resolution: 1.43→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. Residues simultaneously refined in two or more conformations are: Val53, Leu66, Ser86, Lys87, Leu99, Ser110, ...Details: Bulk solvent terms included in Fob file created with standard X-PLOR script. Residues simultaneously refined in two or more conformations are: Val53, Leu66, Ser86, Lys87, Leu99, Ser110, Ser113, Ser130, Lys159, Asp165, Ser166, Ser170, Gln175, Ser217, Lys230, Ser236, Ser244. Disordered waters are: HOH350 which is close to HOH537; HOH749 WHICH IS CLOSE TO HOH811. His40 and HIS91 are MONOPROTONATED ON THE EPSILON NITROGEN. HIS57 is MONOPROTONATED on the delta nitrogen.
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Refinement step | Cycle: LAST / Resolution: 1.43→7.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.43→1.49 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 7.5 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor obs: 0.2 | |||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.382 / Rfactor Rwork: 0.375 |