+Open data
-Basic information
Entry | Database: PDB / ID: 1bqq | ||||||
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Title | CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX | ||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / MATRIX METALLOPROTEINASE / TISSUE INHIBITOR OF METALLOPROTEINASES / PROTEINASE COMPLEX / PRO-GELATINASE A ACTIVATOR / COMPLEX (METALLOPROTEINASE-RECEPTOR) / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information membrane-type matrix metalloproteinase-1 / craniofacial suture morphogenesis / positive regulation of macrophage migration / macropinosome / response to odorant / head development / negative regulation of membrane protein ectodomain proteolysis / chondrocyte proliferation / astrocyte cell migration / tissue remodeling ...membrane-type matrix metalloproteinase-1 / craniofacial suture morphogenesis / positive regulation of macrophage migration / macropinosome / response to odorant / head development / negative regulation of membrane protein ectodomain proteolysis / chondrocyte proliferation / astrocyte cell migration / tissue remodeling / metalloendopeptidase inhibitor activity / negative regulation of focal adhesion assembly / positive regulation of protein processing / endochondral ossification / embryonic cranial skeleton morphogenesis / endothelial cell proliferation / zymogen activation / intermediate filament cytoskeleton / positive regulation of B cell differentiation / branching morphogenesis of an epithelial tube / positive regulation of myotube differentiation / negative regulation of Notch signaling pathway / Activation of Matrix Metalloproteinases / endodermal cell differentiation / metalloaminopeptidase activity / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / regulation of protein localization to plasma membrane / response to mechanical stimulus / ovarian follicle development / Degradation of the extracellular matrix / extracellular matrix organization / response to hormone / extracellular matrix / skeletal system development / response to cytokine / cell motility / lung development / response to organic cyclic compound / protein processing / metalloendopeptidase activity / Golgi lumen / response to estrogen / male gonad development / melanosome / integrin binding / cytoplasmic vesicle / positive regulation of cell growth / angiogenesis / endopeptidase activity / response to oxidative stress / protease binding / response to hypoxia / positive regulation of cell migration / serine-type endopeptidase activity / focal adhesion / proteolysis / extracellular space / zinc ion binding / metal ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.75 Å | ||||||
Authors | Fernandez-Catalan, C. / Bode, W. / Huber, R. / Turk, D. / Calvete, J.J. / Lichte, A. / Tschesche, H. / Maskos, K. | ||||||
Citation | Journal: EMBO J. / Year: 1998 Title: Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. Authors: Fernandez-Catalan, C. / Bode, W. / Huber, R. / Turk, D. / Calvete, J.J. / Lichte, A. / Tschesche, H. / Maskos, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bqq.cif.gz | 89 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bqq.ent.gz | 71.2 KB | Display | PDB format |
PDBx/mmJSON format | 1bqq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bq/1bqq ftp://data.pdbj.org/pub/pdb/validation_reports/bq/1bqq | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 19795.799 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) References: UniProt: P50281, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases | ||||
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#2: Protein | Mass: 20528.699 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Production host: Escherichia coli (E. coli) / References: UniProt: P16368 | ||||
#3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 40 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.6 / Details: pH 5.60 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.6 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 11911 / % possible obs: 97 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Rmerge(I) obs: 0.095 |
Reflection shell | Resolution: 2.5→2.6 Å / Rmerge(I) obs: 0.389 / % possible all: 93.2 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 20 Å / Num. measured all: 73215 |
Reflection shell | *PLUS % possible obs: 93.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.75→20 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.75→20 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.843 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / Num. reflection obs: 8537 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |