+Open data
-Basic information
Entry | Database: PDB / ID: 2jsd | ||||||
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Title | Solution structure of MMP20 complexed with NNGH | ||||||
Components | Matrix metalloproteinase-20 | ||||||
Keywords | HYDROLASE / MMP-NNGH / Structural Genomics / Structural Proteomics in Europe / SPINE / SPINE-2 / SPINE2-COMPLEXES | ||||||
Function / homology | Function and homology information regulation of enamel mineralization / amelogenesis / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / Assembly of collagen fibrils and other multimeric structures / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / extracellular matrix / Degradation of the extracellular matrix / extracellular matrix organization ...regulation of enamel mineralization / amelogenesis / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / Assembly of collagen fibrils and other multimeric structures / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / extracellular matrix / Degradation of the extracellular matrix / extracellular matrix organization / protein catabolic process / metalloendopeptidase activity / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Arendt, Y. / Banci, L. / Bertini, I. / Cantini, F. / Cozzi, R. / Del Conte, R. / Gonnelli, L. / Structural Proteomics in Europe (SPINE) | ||||||
Citation | Journal: Febs Lett. / Year: 2007 Title: Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase. Authors: Arendt, Y. / Banci, L. / Bertini, I. / Cantini, F. / Cozzi, R. / Del Conte, R. / Gonnelli, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jsd.cif.gz | 944.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jsd.ent.gz | 818.1 KB | Display | PDB format |
PDBx/mmJSON format | 2jsd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/js/2jsd ftp://data.pdbj.org/pub/pdb/validation_reports/js/2jsd | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17496.484 Da / Num. of mol.: 1 / Fragment: catalytic domain, residues 113-272 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: Odontoblast / Gene: MMP20 / Plasmid: pET21a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: O60882, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases | ||||
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#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-NGH / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.05 / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 400 / Conformers submitted total number: 20 |