+
Open data
-
Basic information
Entry | Database: PDB / ID: 1c3i | ||||||
---|---|---|---|---|---|---|---|
Title | HUMAN STROMELYSIN-1 CATALYTIC DOMAIN COMPLEXED WITH RO-26-2812 | ||||||
![]() | STROMELYSIN-1 | ||||||
![]() | HYDROLASE / stromelysin-1 / site mutant (GLU202-GLN) | ||||||
Function / homology | ![]() stromelysin 1 / cellular response to UV-A / regulation of neuroinflammatory response / Assembly of collagen fibrils and other multimeric structures / Activation of Matrix Metalloproteinases / response to amyloid-beta / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / cellular response to nitric oxide ...stromelysin 1 / cellular response to UV-A / regulation of neuroinflammatory response / Assembly of collagen fibrils and other multimeric structures / Activation of Matrix Metalloproteinases / response to amyloid-beta / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / cellular response to nitric oxide / negative regulation of reactive oxygen species metabolic process / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / regulation of cell migration / EGFR Transactivation by Gastrin / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / cellular response to amino acid stimulus / protein catabolic process / positive regulation of protein-containing complex assembly / metalloendopeptidase activity / cellular response to reactive oxygen species / metallopeptidase activity / peptidase activity / cellular response to lipopolysaccharide / Interleukin-4 and Interleukin-13 signaling / endopeptidase activity / Extra-nuclear estrogen signaling / serine-type endopeptidase activity / innate immune response / mitochondrion / proteolysis / extracellular space / zinc ion binding / extracellular region / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Steele, D.L. / Kammlott, R.U. / Crowther, R.L. / Birktoft, J.J. / Dunten, P. / Engler, J.E. | ||||||
![]() | ![]() Title: Expression, characterization and structure determination of an active site mutant (Glu202-Gln) of mini-stromelysin-1. Authors: Steele, D.L. / El-Kabbani, O. / Dunten, P. / Windsor, L.J. / Kammlott, R.U. / Crowther, R.L. / Michoud, C. / Engler, J.A. / Birktoft, J.J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 87.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 65.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 735.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 739 KB | Display | |
Data in XML | ![]() | 17 KB | Display | |
Data in CIF | ![]() | 24.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 19416.529 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH SYNTHETIC INHIBITOR (RO-26-2812) BASED ON PRO-PEPTIDE SEQUENCE Source: (gene. exp.) ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-CA / #4: Chemical | ChemComp-TR1 / | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.61 % | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG, POTASSIUM CHLORIDE, CALCIUM CHLORIDE, CACODYLATE, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / PH range low: 7 / PH range high: 6.5 | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Jan 1, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.83 Å / Num. all: 28276 / Num. obs: 20265 / Redundancy: 2.7 % / Rmerge(I) obs: 0.087 / Net I/σ(I): 6.9 |
Reflection | *PLUS % possible obs: 70.6 % |
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.83→20 Å /
| ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.83→20 Å
| ||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||
Refine LS restraints | *PLUS
|