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Open data
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Basic information
Entry | Database: PDB / ID: 1wq1 | ||||||
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Title | RAS-RASGAP COMPLEX | ||||||
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![]() | COMPLEX (GTP-BINDING/GTPASE ACTIVATION) / RAS / GAP / ![]() ![]() | ||||||
Function / homology | ![]() regulation of RNA metabolic process / regulation of actin filament polymerization / potassium channel inhibitor activity / negative regulation of Ras protein signal transduction / negative regulation of cell adhesion / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Scheffzek, K. / Ahmadian, M.R. / Kabsch, W. / Wiesmueller, L. / Lautwein, A. / Schmitz, F. / Wittinghofer, A. | ||||||
![]() | ![]() Title: The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Authors: Scheffzek, K. / Ahmadian, M.R. / Kabsch, W. / Wiesmuller, L. / Lautwein, A. / Schmitz, F. / Wittinghofer, A. #1: ![]() Title: The Interaction of Ras with Gtpase-Activating Proteins Authors: Wittinghofer, A. / Scheffzek, K. / Ahmadian, M.R. #2: ![]() Title: Formation of a Transition-State Analog of the Ras Gtpase Reaction by Ras-Gdp, Tetrafluoroaluminate, and Gtpase-Activating Proteins Authors: Mittal, R. / Ahmadian, M.R. / Goody, R.S. / Wittinghofer, A. #3: ![]() Title: Crystal Structure of the Gtpase-Activating Domain of Human P120Gap and Implications for the Interaction with Ras Authors: Scheffzek, K. / Lautwein, A. / Kabsch, W. / Ahmadian, M.R. / Wittinghofer, A. #4: ![]() Title: Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 A Resolution: Implications for the Mechanism of GTP Hydrolysis Authors: Pai, E.F. / Krengel, U. / Petsko, G.A. / Goody, R.S. / Kabsch, W. / Wittinghofer, A. #5: ![]() Title: A Cytoplasmic Protein Stimulates Normal N-Ras P21 Gtpase, But Does not Affect Oncogenic Mutants Authors: Trahey, M. / Mccormick, F. #6: ![]() Title: Biological and Biochemical Properties of Human Rash Genes Mutated at Codon 61 Authors: Der, C.J. / Finkel, T. / Cooper, G.M. #7: ![]() Title: Biological Properties of Human C-Ha-Ras1 Genes Mutated at Codon 12 Authors: Seeburg, P.H. / Colby, W.W. / Capon, D.J. / Goeddel, D.V. / Levinson, A.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 109.3 KB | Display | ![]() |
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PDB format | ![]() | 86.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 326.8 KB | Display | ![]() |
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Full document | ![]() | 339.1 KB | Display | |
Data in XML | ![]() | 13.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
-Protein , 2 types, 2 molecules RG
#1: Protein | ![]() Mass: 18875.191 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 1 - 166 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 38223.277 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 714 - 1047 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Gene (production host): GENE FRAGMENT OF P120GAP, POSITION 2258 - 3259 Production host: ![]() ![]() ![]() |
-Non-polymers , 4 types, 38 molecules 






#3: Chemical | ChemComp-MG / |
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#4: Chemical | ChemComp-GDP / ![]() |
#5: Chemical | ChemComp-AF3 / ![]() |
#6: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 8 / Details: SEE REF. DESCRIBING THE STRUCTURE, pH 8. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Mar 14, 1997 / Details: FRANKS DOUBLE MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.5→30 Å / Num. obs: 15811 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 41.9 Å2 / Rsym value: 0.06 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2.5→2.6 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1.1 / Rsym value: 0.35 / % possible all: 64 |
Reflection | *PLUS Num. measured all: 35339 / Rmerge(I) obs: 0.066 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: RAS:GPPNP (PDB ENTRY 5P21), GAP-334 (PDB ENTRY 1WER) Resolution: 2.5→30 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
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Displacement parameters | Biso mean: 38.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.61 Å / Rfactor Rfree error: 0.047 / Total num. of bins used: 8
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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