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- PDB-1c5m: 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: 1c5m | ||||||
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Title | STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR | ||||||
![]() | (PROTEIN (COAGULATION FACTOR X)) x 2 | ||||||
![]() | BLOOD CLOTTING / selective / S1 site inhibitor / structure-based drug design / urokinase / trypsin / thrombin | ||||||
Function / homology | ![]() coagulation factor Xa / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of leukocyte chemotaxis / positive regulation of TOR signaling / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation ...coagulation factor Xa / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of leukocyte chemotaxis / positive regulation of TOR signaling / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / Intrinsic Pathway of Fibrin Clot Formation / phospholipid binding / Golgi lumen / blood coagulation / positive regulation of cell migration / endoplasmic reticulum lumen / external side of plasma membrane / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region / plasma membrane 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 | ![]() | 156 KB | Display | ![]() |
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PDB format | ![]() | 123.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 405.1 KB | Display | ![]() |
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Full document | ![]() | 419.9 KB | Display | |
Data in XML | ![]() | 10.8 KB | Display | |
Data in CIF | ![]() | 17.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1c5lC ![]() 1c5nC ![]() 1c5oC ![]() 1c5pC ![]() 1c5qC ![]() 1c5rC ![]() 1c5sC ![]() 1c5tC ![]() 1c5uC ![]() 1c5vC ![]() 1c5wC ![]() 1c5xC ![]() 1c5yC ![]() 1c5zC ![]() 1fxaS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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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 | Mass: 28649.725 Da / Num. of mol.: 1 / Fragment: HEAVY CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein | Mass: 10533.713 Da / Num. of mol.: 1 / Fragment: LIGHT CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 49 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 7.5 Details: crystallization conditions : Crystals of truncated human factor Xa were grown in hanging drops from equal volumes of protein solution (5.0 mg/ml in 20 mM Hepes, 50 mM ammonimum sulfate, pH 8. ...Details: crystallization conditions : Crystals of truncated human factor Xa were grown in hanging drops from equal volumes of protein solution (5.0 mg/ml in 20 mM Hepes, 50 mM ammonimum sulfate, pH 8.0) and well solution (25 % PEG 5K, 0.10 M Hepes, 0.2 M ammonium sulfate, pH 7.5)., VAPOR DIFFUSION | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
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: Mar 4, 1999 / 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: 1.64→70.86 Å / Num. all: 21969 / % possible obs: 60 % / Observed criterion σ(I): 1 / Redundancy: 1.9 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 1.95→2.04 Å / Rmerge(I) obs: 0.265 / Mean I/σ(I) obs: 1.6 / % possible all: 32.2 |
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Processing
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Refinement | Starting model: 1FXA Resolution: 1.95→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: His_F13 Disordered waters are: HOH129 which is ...Details: Bulk solvent terms included in Fob file created with standard X-PLOR script. Residues simultaneously refined in two or more conformations are: His_F13 Disordered waters are: HOH129 which is close to a symmetry-related equivalent of itself; HOH294 which is close to a symmetry-related equivalent of itself; HOH370 which is close to HOH371; HOH487 which is close to HOH490; HOH536 which is close to a symmetry-related equivalent of itself; HOH549 which is close to a symmetry-related equivalent of itself; HOH566 which is close to a symmetry-related equivalent of itself; HOH1123 which is close to a symmetry-related equivalent of itself; Waters whose occupancies are greater than unity may be due to ions more electron rich than water. Those waters with occupancies greater than unity are: HOH7, HOH8, HOH466, HOH536, HOH630, HOH671.
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Refinement step | Cycle: LAST / Resolution: 1.95→7.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→2.04 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: 0.226 | |||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.502 / % reflection Rfree: 10 % / Rfactor Rwork: 0.399 |