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Yorodumi- PDB-1ayk: INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ayk | ||||||
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Title | INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, 30 STRUCTURES | ||||||
Components | COLLAGENASE | ||||||
Keywords | METALLOPROTEASE / MATRIX METALLOPROTEASE / HYDROLASE / GLYCOPROTEIN | ||||||
Function / homology | Function and homology information interstitial collagenase / cellular response to UV-A / protein metabolic process / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / extracellular matrix / Degradation of the extracellular matrix ...interstitial collagenase / cellular response to UV-A / protein metabolic process / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / extracellular matrix / Degradation of the extracellular matrix / extracellular matrix organization / positive regulation of protein-containing complex assembly / metalloendopeptidase activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / peptidase activity / Interleukin-4 and Interleukin-13 signaling / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD | ||||||
Authors | Powers, R. / Moy, F.J. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR. Authors: Moy, F.J. / Chanda, P.K. / Cosmi, S. / Pisano, M.R. / Urbano, C. / Wilhelm, J. / Powers, R. #1: Journal: J.Biomol.NMR / Year: 1997 Title: Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase Authors: Moy, F.J. / Pisano, M.R. / Chanda, P.K. / Urbano, C. / Killar, L.M. / Sung, M.-L. / Powers, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ayk.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1ayk.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 1ayk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ay/1ayk ftp://data.pdbj.org/pub/pdb/validation_reports/ay/1ayk | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 18865.541 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell: FIBROBLAST / Cell line: BL21 / Plasmid: PNOT-3A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P03956, interstitial collagenase | ||
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#2: Chemical | #3: Chemical | ChemComp-CA / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 6.5 / Pressure: 1 atm / Temperature: 308 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX2600 / Manufacturer: Bruker / Model: AMX2600 / Field strength: 600 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY, LOWEST VIOLATIONS, CONSISTENT FOLD Conformers calculated total number: 100 / Conformers submitted total number: 30 |