[English] 日本語
![](img/lk-miru.gif)
- PDB-1cmq: SMALL MOLECULE BINDING TO AN ARTIFICIALLY CREATED CAVITY AT THE A... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1cmq | ||||||
---|---|---|---|---|---|---|---|
Title | SMALL MOLECULE BINDING TO AN ARTIFICIALLY CREATED CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE | ||||||
![]() | CYTOCHROME C PEROXIDASE | ||||||
![]() | OXIDOREDUCTASE(H2O2(A)) | ||||||
Function / homology | ![]() cytochrome-c peroxidase / cytochrome-c peroxidase activity / response to reactive oxygen species / hydrogen peroxide catabolic process / mitochondrial intermembrane space / peroxidase activity / cellular response to oxidative stress / mitochondrial matrix / heme binding / mitochondrion / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Fitzgerald, M.M. / Mcree, D.E. / Churchill, M.J. / Goodin, D.B. | ||||||
![]() | ![]() Title: Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase. Authors: Fitzgerald, M.M. / Churchill, M.J. / McRee, D.E. / Goodin, D.B. #1: ![]() Title: The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential Electronic Structure and Coupling of the Tryptophan Free-Radical to the Heme Authors: Goodin, D.B. / Mcree, D.E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 83.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 63 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 478.8 KB | Display | |
Data in XML | ![]() | 8.6 KB | Display | |
Data in CIF | ![]() | 12.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 33458.258 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: POTENTIAL / References: UniProt: P00431, cytochrome-c peroxidase |
---|---|
#2: Chemical | ChemComp-HEM / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.59 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: vapor diffusion, sitting drop / Details: Wang, J.M. (1990) Biochemistry, 29, 7160. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 19881 / % possible obs: 80 % / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS Mean I/σ(I) obs: 1.7 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→5 Å / σ(F): 0 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→5 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|