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Open data
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Basic information
Entry | Database: PDB / ID: 1ck7 | ||||||
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Title | GELATINASE A (FULL-LENGTH) | ||||||
![]() | PROTEIN (GELATINASE A) | ||||||
![]() | HYDROLASE / HYDROLASE (METALLOPROTEASE) / FULL-LENGTH / METALLOPROTEINASE / GELATINASE A | ||||||
Function / homology | ![]() gelatinase A / peripheral nervous system axon regeneration / blood vessel maturation / parturition / luteinization / bone trabecula formation / tissue remodeling / intramembranous ossification / cellular response to UV-A / ovulation from ovarian follicle ...gelatinase A / peripheral nervous system axon regeneration / blood vessel maturation / parturition / luteinization / bone trabecula formation / tissue remodeling / intramembranous ossification / cellular response to UV-A / ovulation from ovarian follicle / positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / prostate gland epithelium morphogenesis / protein metabolic process / cellular response to fluid shear stress / negative regulation of cell adhesion / face morphogenesis / negative regulation of vasoconstriction / Activation of Matrix Metalloproteinases / endodermal cell differentiation / macrophage chemotaxis / response to amyloid-beta / fibronectin binding / Collagen degradation / collagen catabolic process / EPH-ephrin mediated repulsion of cells / extracellular matrix disassembly / ephrin receptor signaling pathway / response to hyperoxia / cellular response to interleukin-1 / response to electrical stimulus / response to mechanical stimulus / response to retinoic acid / ovarian follicle development / positive regulation of vascular associated smooth muscle cell proliferation / embryo implantation / Degradation of the extracellular matrix / sarcomere / extracellular matrix organization / response to activity / cellular response to estradiol stimulus / cellular response to amino acid stimulus / response to nicotine / protein catabolic process / response to hydrogen peroxide / metalloendopeptidase activity / cellular response to reactive oxygen species / response to estrogen / metallopeptidase activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / heart development / angiogenesis / Interleukin-4 and Interleukin-13 signaling / collagen-containing extracellular matrix / endopeptidase activity / Extra-nuclear estrogen signaling / response to hypoxia / positive regulation of cell migration / response to xenobiotic stimulus / serine-type endopeptidase activity / mitochondrion / proteolysis / extracellular space / zinc ion binding / extracellular region / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Morgunova, E. / Tuuttila, A. / Bergmann, U. / Isupov, M. / Lindqvist, Y. / Schneider, G. / Tryggvason, K. | ||||||
![]() | ![]() Title: Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Authors: Morgunova, E. / Tuuttila, A. / Bergmann, U. / Isupov, M. / Lindqvist, Y. / Schneider, G. / Tryggvason, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 142.8 KB | Display | ![]() |
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PDB format | ![]() | 109.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439 KB | Display | ![]() |
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Full document | ![]() | 495.6 KB | Display | |
Data in XML | ![]() | 32.1 KB | Display | |
Data in CIF | ![]() | 44.4 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 70995.406 Da / Num. of mol.: 1 / Fragment: FULL-LENGTH / Mutation: E404A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 6 types, 113 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-CL / | #5: Chemical | ChemComp-NA / | #6: Chemical | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.49 Å3/Da / Density % sol: 72 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.8 / Details: pH 7.8 | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / 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 | Detector: CCD / Date: Oct 1, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97984 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→34 Å / Num. obs: 32057 / % possible obs: 99.7 % / Redundancy: 10.2 % / Biso Wilson estimate: 105 Å2 / Rsym value: 0.117 / Net I/σ(I): 20.9 |
Reflection shell | Resolution: 2.8→2.98 Å / Redundancy: 10.5 % / Mean I/σ(I) obs: 2 / Rsym value: 0.403 / % possible all: 95.4 |
Reflection | *PLUS Num. measured all: 333608 / Rmerge(I) obs: 0.117 |
Reflection shell | *PLUS % possible obs: 99.7 % / Rmerge(I) obs: 0.402 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1GEN, PDB ENTRY 1FBL Resolution: 2.8→34 Å / σ(F): 0 Details: NO ELECTRON DENSITY WAS OBSERVED FOR THE N-TERMINAL RESIDUE ALA 30 AND FOR RESIDUES ASP 450 - THR 460. PRESUMABLY THEY ARE DISORDERED. THESE RESIDUES ARE PART OF A FLEXIBLE LINKAGE BETWEEN ...Details: NO ELECTRON DENSITY WAS OBSERVED FOR THE N-TERMINAL RESIDUE ALA 30 AND FOR RESIDUES ASP 450 - THR 460. PRESUMABLY THEY ARE DISORDERED. THESE RESIDUES ARE PART OF A FLEXIBLE LINKAGE BETWEEN CATALYTIC CORE AND C-TERMINAL HEMOPEXIN PARTS OF MMP-2. RESIDUES 108 - 116 WERE MODELED INTO POOR ELECTRON DENSITY. THE SIDE CHAIN ORIENTATIONS WERE TAKEN FROM THE ROTAMER LIBRARY. THESE RESIDUES ARE IN THE LOOP WHICH CONECTS PROPEPTIDE AND CATALYTIC DOMAIN. THE ELECTRON DENSITY FOR THE SURFACE LOOP 649 - 652 IS WEAK, AND THE INDIVIDUAL B-FACTORS ARE RATHER HIGH.
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Displacement parameters | Biso mean: 63.5 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→34 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 34 Å / % reflection Rfree: 5 % / Rfactor obs: 0.286 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 63.5 Å2 |