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- PDB-2ozr: MMP13 Catalytic Domain Complexed with 4-{[1-methyl-2,4-dioxo-6-(3... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ozr | ||||||
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Title | MMP13 Catalytic Domain Complexed with 4-{[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl}benzoic acid | ||||||
![]() | Collagenase 3 | ||||||
![]() | HYDROLASE / Crystal Complex Structure / Matrix Metalloproteinase / MMP13 Catalytic Domain / MMP13 Specific Inhibitor | ||||||
Function / homology | ![]() growth plate cartilage development / RUNX2 regulates genes involved in cell migration / endochondral ossification / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / bone morphogenesis / Assembly of collagen fibrils and other multimeric structures / bone mineralization / Activation of Matrix Metalloproteinases / response to amyloid-beta / Collagen degradation ...growth plate cartilage development / RUNX2 regulates genes involved in cell migration / endochondral ossification / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / bone morphogenesis / Assembly of collagen fibrils and other multimeric structures / bone mineralization / Activation of Matrix Metalloproteinases / response to amyloid-beta / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / collagen binding / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / metalloendopeptidase activity / endopeptidase activity / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Johnson, A.R. / Pavlovsky, A.G. / Ortwine, D.F. / Prior, F. / Man, C.-F. / Bornemeier, D.A. / Banotai, C.A. / Mueller, W.T. / McConnell, P. / Yan, C.H. ...Johnson, A.R. / Pavlovsky, A.G. / Ortwine, D.F. / Prior, F. / Man, C.-F. / Bornemeier, D.A. / Banotai, C.A. / Mueller, W.T. / McConnell, P. / Yan, C.H. / Baragi, V. / Lesch, C. / Roark, W.H. / Lie, J.J. / Fasquelle, V. / Wilson, M. / Robertson, D. / Datta, K. / Guzman, R. / Han, H.-K. / Dyer, R.D. | ||||||
![]() | ![]() Title: Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects. Authors: Johnson, A.R. / Pavlovsky, A.G. / Ortwine, D.F. / Prior, F. / Man, C.F. / Bornemeier, D.A. / Banotai, C.A. / Mueller, W.T. / McConnell, P. / Yan, C. / Baragi, V. / Lesch, C. / Roark, W.H. / ...Authors: Johnson, A.R. / Pavlovsky, A.G. / Ortwine, D.F. / Prior, F. / Man, C.F. / Bornemeier, D.A. / Banotai, C.A. / Mueller, W.T. / McConnell, P. / Yan, C. / Baragi, V. / Lesch, C. / Roark, W.H. / Wilson, M. / Datta, K. / Guzman, R. / Han, H.K. / Dyer, R.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 305 KB | Display | ![]() |
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PDB format | ![]() | 247 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.4 MB | Display | ![]() |
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Full document | ![]() | 2.4 MB | Display | |
Data in XML | ![]() | 63.8 KB | Display | |
Data in CIF | ![]() | 88.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ow9SC 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Refine code: 4
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Components
-Protein , 1 types, 8 molecules ABCDEFGH
#1: Protein | Mass: 19069.314 Da / Num. of mol.: 8 / Fragment: Catalytic Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P45452, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases |
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-Non-polymers , 5 types, 1076 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/GG1.gif)
![](data/chem/img/HAE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/GG1.gif)
![](data/chem/img/HAE.gif)
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#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-CA / #4: Chemical | ChemComp-GG1 / #5: Chemical | ChemComp-HAE / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.44 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Dissolved in DMSO inhibitor was mixed with protein (protein concentration: 1mg/ml) at 5:1 ratio, 0.1 M acetohydrohamic acid added. Ternary complex was concentrated (to 17 mg/ml protien ...Details: Dissolved in DMSO inhibitor was mixed with protein (protein concentration: 1mg/ml) at 5:1 ratio, 0.1 M acetohydrohamic acid added. Ternary complex was concentrated (to 17 mg/ml protien concentration). 1-2 uL hagind drops were mixed with same amount of reservoit solution (2.1 M ammonium sulfate in 0.1 M Hepes buffer) , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 25, 2001 / Details: mirrors |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. all: 160245 / Num. obs: 69624 / % possible obs: 90.7 % / Redundancy: 2.3 % / Biso Wilson estimate: 26 Å2 / Rsym value: 0.096 / Χ2: 1.433 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 2.1→2.18 Å / Mean I/σ(I) obs: 2 / Num. unique all: 4793 / Rsym value: 0.342 / Χ2: 0.991 / % possible all: 62.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB Entry 2OW9 Resolution: 2.3→50 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.898 / SU B: 18.324 / SU ML: 0.264 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.841 / ESU R Free: 0.38 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: Used NCS Restraints
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.737 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→50 Å
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Refine LS restraints |
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Refine LS restraints NCS | Ens-ID: 1 / Number: 1279 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.3→2.36 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 20.4251 Å / Origin y: 0.0314 Å / Origin z: 28.1447 Å
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Refinement TLS group | Refine-ID: X-RAY DIFFRACTION / Refine TLS-ID: 1 / Selection: ALL
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