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Yorodumi- PDB-5uwk: Matrix metalloproteinase-13 complexed with selective inhibitor co... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5uwk | ||||||
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Title | Matrix metalloproteinase-13 complexed with selective inhibitor compound (S)-10a | ||||||
Components | Collagenase 3 | ||||||
Keywords | hydrolase/hydrolase inhibitor / Metalloproteinase / collagenase / MMP-13 / hydrolase / hydrolase-hydrolase inhibitor complex | ||||||
Function / homology | Function and homology information 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 | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Taylor, A.B. / Cao, X. / Hart, P.J. | ||||||
Citation | Journal: J. Med. Chem. / Year: 2017 Title: Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors. Authors: Choi, J.Y. / Fuerst, R. / Knapinska, A.M. / Taylor, A.B. / Smith, L. / Cao, X. / Hart, P.J. / Fields, G.B. / Roush, W.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5uwk.cif.gz | 157.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5uwk.ent.gz | 120.4 KB | Display | PDB format |
PDBx/mmJSON format | 5uwk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5uwk_validation.pdf.gz | 891.3 KB | Display | wwPDB validaton report |
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Full document | 5uwk_full_validation.pdf.gz | 894.2 KB | Display | |
Data in XML | 5uwk_validation.xml.gz | 18.6 KB | Display | |
Data in CIF | 5uwk_validation.cif.gz | 27.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uw/5uwk ftp://data.pdbj.org/pub/pdb/validation_reports/uw/5uwk | HTTPS FTP |
-Related structure data
Related structure data | 5uwlC 5uwmC 5uwnC 4l19S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 19366.578 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: CATALYTIC DOMAIN (UNP RESIDUES 104-274) / Source: (gene. exp.) Homo sapiens (human) / Gene: MMP13 / Plasmid: PKA8H / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P45452, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-CA / #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 39.6 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.2 M magnesium chloride, 0.1 M Tris:HCl pH 8.5, 25% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 14, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→120.56 Å / Num. obs: 42491 / % possible obs: 99.7 % / Redundancy: 3.9 % / Biso Wilson estimate: 18.2 Å2 / Rpim(I) all: 0.035 / Rsym value: 0.062 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 4 % / Mean I/σ(I) obs: 1.9 / Num. unique obs: 6124 / Rpim(I) all: 0.43 / Rsym value: 0.768 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4L19 Resolution: 1.6→51.646 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 19.44
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→51.646 Å
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Refine LS restraints |
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LS refinement shell |
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