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- PDB-1fbl: STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fbl | ||||||
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Title | STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER | ||||||
![]() | FIBROBLAST (INTERSTITIAL) COLLAGENASE (MMP-1) | ||||||
![]() | METALLOPROTEASE | ||||||
Function / homology | ![]() Collagen degradation / Activation of Matrix Metalloproteinases / Degradation of the extracellular matrix / interstitial collagenase / Basigin interactions / collagen catabolic process / extracellular matrix organization / extracellular matrix / metalloendopeptidase activity / peptidase activity ...Collagen degradation / Activation of Matrix Metalloproteinases / Degradation of the extracellular matrix / interstitial collagenase / Basigin interactions / collagen catabolic process / extracellular matrix organization / extracellular matrix / metalloendopeptidase activity / peptidase activity / serine-type endopeptidase activity / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Li, J. / Brick, P. / Blow, D.M. | ||||||
![]() | ![]() Title: Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller. Authors: Li, J. / Brick, P. / O'Hare, M.C. / Skarzynski, T. / Lloyd, L.F. / Curry, V.A. / Clark, I.M. / Bigg, H.F. / Hazleman, B.L. / Cawston, T.E. / Blow, D.M. #1: ![]() Title: Crystallization and Preliminary X-Ray Analysis of Porcine Synovial Collagenase Authors: Lloyd, L.F. / Skarzynski, T. / Wonacott, A.J. / Cawston, T.E. / Clark, I.M. / Mannix, C.J. / Harper, G.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 92.4 KB | Display | ![]() |
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PDB format | ![]() | 73.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 771.8 KB | Display | ![]() |
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Full document | ![]() | 781.2 KB | Display | |
Data in XML | ![]() | 19.8 KB | Display | |
Data in CIF | ![]() | 29.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 42688.355 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||||||
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#2: Chemical | ChemComp-CA / #3: Chemical | #4: Chemical | ChemComp-HTA / | #5: Water | ChemComp-HOH / | Compound details | THE ENZYME CONSISTS OF AN N-TERMINAL CATALYTIC DOMAIN JOINED BY A LINKING PEPTIDE TO A C-TERMINAL ...THE ENZYME CONSISTS OF AN N-TERMINAL CATALYTIC DOMAIN JOINED BY A LINKING PEPTIDE TO A C-TERMINAL DOMAIN. THE MODEL FOR THE N-TERMINAL DOMAIN (RESIDUES 100 - 260) INCLUDES TWO ZINC IONS AND 3 CALCIUM IONS. ZINC 998 IS AT THE ACTIVE SITE AND COORDINATE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.97 Å3/Da / Density % sol: 69.01 % | ||||||||||||||||||
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Crystal | *PLUS Density % sol: 70.5 % | ||||||||||||||||||
Crystal grow | *PLUS pH: 7.3 / Method: vapor diffusion, hanging drop | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Oct 11, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.876 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→42.2 Å / Num. obs: 22212 / % possible obs: 94.2 % / Redundancy: 3.27 % / Rmerge(I) obs: 0.086 |
Reflection | *PLUS Num. measured all: 72655 / Rmerge(I) obs: 0.086 |
Reflection shell | *PLUS % possible obs: 66.7 % / Rmerge(I) obs: 0.23 |
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Processing
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Refinement | Resolution: 2.5→9 Å / σ(F): 0 Details: THE CONFORMATION OF THE MAIN CHAIN IS NOT WELL DEFINED FOR RESIDUES 263 - 268, 306 - 311 AND 402 - 409.
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Displacement parameters | Biso mean: 34.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→9 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.61 Å / Rfactor obs: 0.366 |