+
Open data
-
Basic information
Entry | Database: PDB / ID: 5fow | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | HUMANISED MONOMERIC RADA IN COMPLEX WITH WHTA TETRAPEPTIDE | |||||||||
![]() |
| |||||||||
![]() | HYDROLASE / RADA / FXXA MOTIF / RECOMBINASE | |||||||||
Function / homology | ![]() DNA recombinase assembly / mitotic recombination / DNA strand invasion / DNA strand exchange activity / ATP-dependent DNA damage sensor activity / single-stranded DNA binding / double-stranded DNA binding / damaged DNA binding / ATP hydrolysis activity / ATP binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Scott, D.E. / Marsh, M. / Blundell, T.L. / Abell, C. / Hyvonen, M. | |||||||||
![]() | ![]() Title: Structure Activity Relationship of the Peptide Binding Motif Mediating the Rad51:Brca2 Protein-Protein Interaction. Authors: Scott, D.E. / Marsh, M. / Blundell, T.L. / Abell, C. / Hyvonen, M. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 199.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 157.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 456.2 KB | Display | |
Data in XML | ![]() | 24.9 KB | Display | |
Data in CIF | ![]() | 37.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5fotC ![]() 5fouC ![]() 5fovC ![]() 5foxC ![]() 5fpkC ![]() 4b3bS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 25502.150 Da / Num. of mol.: 2 / Fragment: ATPASE, UNP RESIDUES 108-349 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / Gene: radA, PF1926 / Plasmid: PBAT4 / Production host: ![]() ![]() #2: Protein/peptide | Mass: 538.599 Da / Num. of mol.: 2 / Source method: obtained synthetically Details: ACETYLATED AT THE N-TERMINUS AND AMIDATED IN THE C-TERMINUS Source: (synth.) ![]() #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | MUTATIONS I169M, Y201A, V202Y, K221M AND REPLACEMEN | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.1 % / Description: NONE |
---|---|
Crystal grow | pH: 6.2 / Details: 8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jan 23, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97952 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→33.23 Å / Num. obs: 38505 / % possible obs: 95.7 % / Observed criterion σ(I): 3 / Redundancy: 2.79 % / Biso Wilson estimate: 21.2 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 9.96 |
Reflection shell | Resolution: 1.8→1.91 Å / Redundancy: 2.76 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 3.05 / % possible all: 93.5 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4B3B Resolution: 1.797→33.232 Å / SU ML: 0.2 / σ(F): 2 / Phase error: 22.5 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.9 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.797→33.232 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS group |
|