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- PDB-1cqr: CRYSTAL STRUCTURE OF THE STROMELYSIN CATALYTIC DOMAIN AT 2.0 A RE... -
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Basic information
Entry | Database: PDB / ID: 1cqr | ||||||
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Title | CRYSTAL STRUCTURE OF THE STROMELYSIN CATALYTIC DOMAIN AT 2.0 A RESOLUTION | ||||||
![]() | STROMELYSIN-1 | ||||||
![]() | HYDROLASE / ACTIVE / TRUNCATED NATIVE ENZYME | ||||||
Function / homology | ![]() stromelysin 1 / cellular response to UV-A / regulation of neuroinflammatory response / Assembly of collagen fibrils and other multimeric structures / Activation of Matrix Metalloproteinases / response to amyloid-beta / Collagen degradation / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / collagen catabolic process / cellular response to nitric oxide ...stromelysin 1 / cellular response to UV-A / regulation of neuroinflammatory response / Assembly of collagen fibrils and other multimeric structures / Activation of Matrix Metalloproteinases / response to amyloid-beta / Collagen degradation / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / collagen catabolic process / cellular response to nitric oxide / negative regulation of reactive oxygen species metabolic process / extracellular matrix disassembly / EGFR Transactivation by Gastrin / regulation of cell migration / Degradation of the extracellular matrix / extracellular matrix / extracellular matrix organization / cellular response to amino acid stimulus / positive regulation of protein-containing complex assembly / protein catabolic process / metalloendopeptidase activity / cellular response to reactive oxygen species / metallopeptidase activity / peptidase activity / cellular response to lipopolysaccharide / Interleukin-4 and Interleukin-13 signaling / endopeptidase activity / Extra-nuclear estrogen signaling / serine-type endopeptidase activity / innate immune response / mitochondrion / proteolysis / extracellular space / zinc ion binding / extracellular region / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Chen, L. / Rydel, T.J. / Gu, F. / Dunaway, C.M. / Pikul, S. / Dunham, K.M. / Barnett, B.L. | ||||||
![]() | ![]() Title: Crystal structure of the stromelysin catalytic domain at 2.0 A resolution: inhibitor-induced conformational changes. Authors: Chen, L. / Rydel, T.J. / Gu, F. / Dunaway, C.M. / Pikul, S. / Dunham, K.M. / Barnett, B.L. #1: ![]() Title: Design and Synthesis of Phosphinamide-Based Hydroxamic Acids as Inhibitors of Matrix Metalloproteinases Authors: Pikul, S. / McDow Dunham, K.L. / Almstead, N.G. / De, B. / Natchus, M.G. / Anastasio, M.V. / McPhail, S.J. / Snider, C.E. / Taiwo, Y.O. / Chen, L. / Dunaway, C.M. / Gu, F. / Mieling, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 84.2 KB | Display | ![]() |
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PDB format | ![]() | 63.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 |
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Unit cell |
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Details | The biological assembly is a monomer |
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Components
#1: Protein | Mass: 19416.529 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-CA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.08 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 20-24% PEG 8000, 2.5% 2-propanol, 10mM CaCl2, 0.1 M Tris-HCL buffer, VAPOR DIFFUSION, HANGING DROP, temperature 298.K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / PH range low: 8.5 / PH range high: 7.5 | ||||||||||||||||||||||||||||||||||||
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 II / Detector: IMAGE PLATE / Date: May 24, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→12 Å / Num. all: 24377 / Num. obs: 21471 / % possible obs: 94.7 % / Observed criterion σ(F): 2 / Redundancy: 4.3 % / Biso Wilson estimate: 12.7 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 2→12 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.058 / Num. unique all: 24377 / % possible all: 94.7 |
Reflection shell | *PLUS % possible obs: 94.7 % |
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Processing
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Refinement | Resolution: 2→12 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 1 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→12 Å
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Refine LS restraints |
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