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- PDB-1ffh: N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN F... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ffh | ||||||
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Title | N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS | ||||||
![]() | FFH | ||||||
![]() | RIBONUCLEOPROTEIN / FFH / SRP / GTPASE / SIGNAL RECOGNITION PARTICLE | ||||||
Function / homology | ![]() signal recognition particle / endoplasmic reticulum signal peptide binding / signal-recognition-particle GTPase / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane, translocation / GTPase activity / GTP binding / ATP hydrolysis activity / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Freymann, D.M. / Keenan, R.J. / Stroud, R.M. / Walter, P. | ||||||
![]() | ![]() Title: Structure of the conserved GTPase domain of the signal recognition particle. Authors: Freymann, D.M. / Keenan, R.J. / Stroud, R.M. / Walter, 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 | ![]() | 69.7 KB | Display | ![]() |
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PDB format | ![]() | 51.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 413.3 KB | Display | ![]() |
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Full document | ![]() | 414.3 KB | Display | |
Data in XML | ![]() | 13 KB | Display | |
Data in CIF | ![]() | 18 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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Unit cell |
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Components
#1: Protein | Mass: 32256.250 Da / Num. of mol.: 1 / Fragment: 'NG' GTPASE FRAGMENT OF FFH Source method: isolated from a genetically manipulated source Details: THE NG FRAGMENT WAS GENERATED BY PROTEOLYSIS / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Water | ChemComp-HOH / |
Sequence details | FEATURES IN THE FO-FC MAP SUGGEST THAT ALA 48 (BASED ON THE SEQUENCE OF THE T. AQUATICUS FFH GENE) ...FEATURES IN THE FO-FC MAP SUGGEST THAT ALA 48 (BASED ON THE SEQUENCE OF THE T. AQUATICUS FFH GENE) IS THR, SER, OR VAL IN THIS STRUCTURE. THE EXPRESSION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.79 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, sitting drop / pH: 9 Details: PROTEIN AT 30 MG/ML IN WATER. CRYSTALLIZED AT RT BY SITTING DROP VAPOR DIFFUSION USING 30% PEG MME 550, 50 MM TAPS PH 9.0, 200 MM MGCL2., vapor diffusion - sitting drop | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting 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: Mar 19, 1996 / Details: SUPPER DOUBLE MIRRORS |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.05 Å / Num. obs: 16644 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 13.2 Å2 / Rsym value: 0.046 |
Reflection shell | Resolution: 2.05→2.12 Å / Redundancy: 3.9 % / Rsym value: 0.137 / % possible all: 98.4 |
Reflection | *PLUS Rmerge(I) obs: 0.046 |
Reflection shell | *PLUS % possible obs: 98.4 % / Rmerge(I) obs: 0.137 |
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Processing
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Refinement | Method to determine structure: ![]() Details: THE ELECTRON DENSITY FOR THE TURN COMPRISING THESE RESIDUES IS NOT YET CORRECTLY MODELED: THR 23, GLU 24, GLU 25.
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Displacement parameters | Biso mean: 21.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.05→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.05→2.11 Å / Total num. of bins used: 12
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Xplor file |
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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 Rfactor obs: 0.248 |