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- PDB-1cge: CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cge | ||||||
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Title | CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF | ||||||
![]() | FIBROBLAST COLLAGENASE | ||||||
![]() | HYDROLASE (METALLOPROTEASE) | ||||||
Function / homology | ![]() interstitial collagenase / cellular response to UV-A / protein metabolic process / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization ...interstitial collagenase / cellular response to UV-A / protein metabolic process / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / 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 | ![]() | ||||||
Method | ![]() | ||||||
![]() | Lovejoy, B. / Hassell, A.M. / Luther, M.A. / Weigl, D. / Jordan, S.R. | ||||||
![]() | ![]() Title: Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Authors: Lovejoy, B. / Hassell, A.M. / Luther, M.A. / Weigl, D. / Jordan, S.R. #1: ![]() Title: Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with an Inhibitor Authors: Lovejoy, B. / Cleasby, A. / Hassell, A.M. / Longley, K. / Luther, M.A. / Weigl, D. / Mcgeehan, G. / Mcelroy, A.B. / Drewry, D. / Lambert, M.H. / Jordan, S.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.9 KB | Display | ![]() |
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PDB format | ![]() | 41.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 364.2 KB | Display | ![]() |
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Full document | ![]() | 366.5 KB | Display | |
Data in XML | ![]() | 5.2 KB | Display | |
Data in CIF | ![]() | 7.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 18822.498 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||||||
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#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE WAS DERIVED FROM THE CDNA SEQUENCE OF G. I. GOLDBERG, ET AL., J. BIOL. CHEM. 261: 6600- ...THE SEQUENCE WAS DERIVED FROM THE CDNA SEQUENCE OF G. I. GOLDBERG, ET AL., J. BIOL. CHEM. 261: 6600-660 (1986), AND DESCRIBED IN THE JRNL REFERENCE ABOVE. N-TERMINAL MASS SPECTROMET | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.18 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion / PH range low: 9 / PH range high: 7 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 13611 / % possible obs: 81.9 % / Rmerge(I) obs: 0.073 |
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Processing
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Refinement | Resolution: 1.9→7 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.9→7 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2 |