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- PDB-1t32: A Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chyma... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1t32 | ||||||
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Title | A Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase with Therapeutic Efficacy in Animals Models of Inflammation | ||||||
![]() | Cathepsin G | ||||||
![]() | HYDROLASE / INFLAMMATION INHIBITOR SERINE PROTEASE | ||||||
Function / homology | ![]() cathepsin G / biofilm matrix disassembly / neutrophil-mediated killing of gram-positive bacterium / purinergic nucleotide receptor signaling pathway / negative regulation of T cell activation / caspase binding / Suppression of apoptosis / protein metabolic process / neutrophil activation / positive regulation of platelet aggregation ...cathepsin G / biofilm matrix disassembly / neutrophil-mediated killing of gram-positive bacterium / purinergic nucleotide receptor signaling pathway / negative regulation of T cell activation / caspase binding / Suppression of apoptosis / protein metabolic process / neutrophil activation / positive regulation of platelet aggregation / Interleukin-1 processing / Antimicrobial peptides / Activation of Matrix Metalloproteinases / monocyte chemotaxis / extracellular matrix disassembly / angiotensin maturation / defense response to fungus / Metabolism of Angiotensinogen to Angiotensins / Purinergic signaling in leishmaniasis infection / Degradation of the extracellular matrix / serine-type peptidase activity / secretory granule / protein processing / platelet activation / cytokine-mediated signaling pathway / cytoplasmic stress granule / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of immune response / azurophil granule lumen / heparin binding / peptidase activity / antibacterial humoral response / cellular response to lipopolysaccharide / collagen-containing extracellular matrix / defense response to Gram-negative bacterium / receptor ligand activity / lysosome / defense response to Gram-positive bacterium / immune response / protein phosphorylation / intracellular membrane-bounded organelle / serine-type endopeptidase activity / Neutrophil degranulation / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | de Garavilla, L. / Greco, M.N. / Giardino, E.C. / Wells, G.I. / Haertlein, B.J. / Kauffman, J.A. / Corcoran, T.W. / Derian, C.K. / Eckardt, A.J. / Abraham, W.M. ...de Garavilla, L. / Greco, M.N. / Giardino, E.C. / Wells, G.I. / Haertlein, B.J. / Kauffman, J.A. / Corcoran, T.W. / Derian, C.K. / Eckardt, A.J. / Abraham, W.M. / Sukumar, N. / Chen, Z. / Pineda, A.O. / Mathews, F.S. / Di Cera, E. / Andrade-Gordon, P. / Damiano, B.P. / Maryanoff, B.E. | ||||||
![]() | ![]() Title: A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo. Authors: de Garavilla, L. / Greco, M.N. / Sukumar, N. / Chen, Z.W. / Pineda, A.O. / Mathews, F.S. / Di Cera, E. / Giardino, E.C. / Wells, G.I. / Haertlein, B.J. / Kauffman, J.A. / Corcoran, T.W. / ...Authors: de Garavilla, L. / Greco, M.N. / Sukumar, N. / Chen, Z.W. / Pineda, A.O. / Mathews, F.S. / Di Cera, E. / Giardino, E.C. / Wells, G.I. / Haertlein, B.J. / Kauffman, J.A. / Corcoran, T.W. / Derian, C.K. / Eckardt, A.J. / Damiano, B.P. / Andrade-Gordon, P. / Maryanoff, B.E. #1: ![]() Title: The 1.8 A crystal structure of human cathepsin G in complex with SUC-VAL-PRO-PHEP-(OPH)2: A Janus-Faced proteinase with two opposite specificities Authors: Hof, P. / Mayr, I. / Huber, R. / Korzus, E. / Potempa, J. / Travis, J. / Powers, J.C. / Bode, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 68.4 KB | Display | ![]() |
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PDB format | ![]() | 48.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 794.6 KB | Display | ![]() |
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Full document | ![]() | 804.2 KB | Display | |
Data in XML | ![]() | 14.9 KB | Display | |
Data in CIF | ![]() | 21.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1t31C ![]() 1cghS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 25484.211 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-OHH / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 35 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion / pH: 7 Details: PEG 4000, Sodium Hepes, sodium acetate, ammonium sulfate, 2-propanol, pH 7.0, VAPOR DIFFUSION, temperature 296.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 30, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→30 Å / Num. all: 17366 / Num. obs: 15108 / % possible obs: 87 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 5.1 % / Biso Wilson estimate: 9 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 22.7 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.199 / Mean I/σ(I) obs: 4 / Num. unique all: 1666 / % possible all: 51.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1CGH Resolution: 1.85→30 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 17.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.85→30 Å
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Refine LS restraints |
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LS refinement shell |
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