+Open data
-Basic information
Entry | Database: PDB / ID: 1mmr | ||||||
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Title | MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR | ||||||
Components | MATRILYSIN | ||||||
Keywords | METALLOPROTEASE | ||||||
Function / homology | Function and homology information matrilysin / antibacterial peptide secretion / antibacterial peptide biosynthetic process / membrane protein intracellular domain proteolysis / Assembly of collagen fibrils and other multimeric structures / Activation of Matrix Metalloproteinases / membrane protein ectodomain proteolysis / Collagen degradation / collagen catabolic process / extracellular matrix disassembly ...matrilysin / antibacterial peptide secretion / antibacterial peptide biosynthetic process / membrane protein intracellular domain proteolysis / Assembly of collagen fibrils and other multimeric structures / Activation of Matrix Metalloproteinases / membrane protein ectodomain proteolysis / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / metalloendopeptidase activity / metallopeptidase activity / regulation of cell population proliferation / defense response to Gram-negative bacterium / endopeptidase activity / Extra-nuclear estrogen signaling / defense response to Gram-positive bacterium / positive regulation of cell migration / response to xenobiotic stimulus / serine-type endopeptidase activity / proteolysis / extracellular space / zinc ion binding / extracellular exosome / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Browner, M.F. / Smith, W.W. / Castelhano, A.L. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Matrilysin-inhibitor complexes: common themes among metalloproteases. Authors: Browner, M.F. / Smith, W.W. / Castelhano, A.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mmr.cif.gz | 48.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mmr.ent.gz | 33.4 KB | Display | PDB format |
PDBx/mmJSON format | 1mmr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mmr_validation.pdf.gz | 458.5 KB | Display | wwPDB validaton report |
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Full document | 1mmr_full_validation.pdf.gz | 459 KB | Display | |
Data in XML | 1mmr_validation.xml.gz | 5.7 KB | Display | |
Data in CIF | 1mmr_validation.cif.gz | 8.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mm/1mmr ftp://data.pdbj.org/pub/pdb/validation_reports/mm/1mmr | HTTPS FTP |
-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: 18741.912 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: OVARY / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P09237, matrilysin | ||||||
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#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-SRS / | #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: 2.59 Å3/Da / Density % sol: 52.59 % | ||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 50.5 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17-25 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 22, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 7690 / % possible obs: 95.5 % / Observed criterion σ(I): 2.5 / Redundancy: 3 % / Rmerge(I) obs: 0.08 |
Reflection | *PLUS Highest resolution: 2.3 Å / Num. measured all: 23346 / Rmerge(I) obs: 0.08 |
-Processing
Software |
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Refinement | Resolution: 2.4→6 Å / σ(F): 0 /
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |