[English] 日本語
![](img/lk-miru.gif)
- PDB-1efv: THREE-DIMENSIONAL STRUCTURE OF HUMAN ELECTRON TRANSFER FLAVOPROTE... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1efv | ||||||
---|---|---|---|---|---|---|---|
Title | THREE-DIMENSIONAL STRUCTURE OF HUMAN ELECTRON TRANSFER FLAVOPROTEIN TO 2.1 A RESOLUTION | ||||||
![]() | (ELECTRON TRANSFER FLAVOPROTEIN) x 2 | ||||||
![]() | ELECTRON TRANSPORT / FLAVOPROTEIN / GLUTARIC ACIDEMIA TYPE II | ||||||
Function / homology | ![]() electron transfer flavoprotein complex / fatty acid beta-oxidation using acyl-CoA dehydrogenase / Respiratory electron transport / amino acid catabolic process / Protein methylation / respiratory electron transport chain / flavin adenine dinucleotide binding / oxidoreductase activity / electron transfer activity / mitochondrial matrix ...electron transfer flavoprotein complex / fatty acid beta-oxidation using acyl-CoA dehydrogenase / Respiratory electron transport / amino acid catabolic process / Protein methylation / respiratory electron transport chain / flavin adenine dinucleotide binding / oxidoreductase activity / electron transfer activity / mitochondrial matrix / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Roberts, D.L. / Frerman, F.E. / Kim, J.J.P. | ||||||
![]() | ![]() Title: Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution. Authors: Roberts, D.L. / Frerman, F.E. / Kim, J.J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 128 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 96.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 532.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 539.4 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 21.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 33134.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: COFACTORS FAD 1 AND AMP 1 ARE NON-COVALENTLY BOUND / Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 27885.646 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: COFACTORS FAD 1 AND AMP 1 ARE NON-COVALENTLY BOUND / Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-FAD / |
#4: Chemical | ChemComp-AMP / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Method: vapor diffusion, sitting drop / pH: 7 Details: THE PROTEIN WAS CRYSTALLIZED FROM 15 % PEG 1500, 50 MM HEPES, PH 7.0. EQUAL VOLUMES OF PROTEIN (15 MG/ML) AND PRECIPITANT WERE MIXED IN SITTING DROPS., vapor diffusion - sitting drop | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 277 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Apr 1, 1994 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 32383 / % possible obs: 96 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rmerge(I) obs: 0.064 / Rsym value: 0.064 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.1→2.14 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.064 / Mean I/σ(I) obs: 2.6 / Rsym value: 0.304 / % possible all: 92.4 |
Reflection | *PLUS % possible obs: 95.6 % / Num. measured all: 118435 |
Reflection shell | *PLUS % possible obs: 92.4 % / Rmerge(I) obs: 0.304 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.1→2.19 Å / Total num. of bins used: 8
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.171 / Rfactor Rfree: 0.221 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor obs: 0.218 |