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Open data
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Basic information
Entry | Database: PDB / ID: 1rax | ||||||
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Title | RA-DOMAIN OF RAL GUANOSINE-NUCLEOTIDE DISSOCIATION STIMULATOR | ||||||
![]() | PROTEIN (RA-DOMAIN OF RAL GUANOSINE DISSOCIATION STIMULATOR) | ||||||
![]() | RAS-BINDING DOMAIN / RALGEF / ![]() | ||||||
Function / homology | ![]() GTPase regulator activity / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mueller, T.D. / Handel, L. / Schmieder, P. / Oschkinat, H. | ||||||
![]() | ![]() Title: High-Resolution Structure of the Ra-Domain of Human Ralgds and a Dynamics Study of its Binding Loop to Ras Authors: Mueller, T.D. / Handel, L. / Schmieder, P. / Oschkinat, H. #1: ![]() Title: Three-dimensional structure of the Ras-interacting domain of RalGDS. Authors: Huang, L. / Weng, X. / Hofer, F. / Martin, G.S. / Kim, S.H. #2: ![]() Title: Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling. Authors: Geyer, M. / Herrmann, C. / Wohlgemuth, S. / Wittinghofer, A. / Kalbitzer, H.R. #3: Journal: J.Biol.Chem. / Year: 1996 Title: Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. Authors: Herrmann, C. / Horn, G. / Spaargaren, M. / Wittinghofer, A. #4: Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Authors: Spaargaren, M. / Bischoff, J.R. #5: Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator. Authors: Hofer, F. / Fields, S. / Schneider, C. / Martin, G.S. #6: Journal: Embo J. / Year: 1993 Title: Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase. Authors: Albright, C.F. / Giddings, B.W. / Liu, J. / Vito, M. / Weinberg, R.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 299.3 KB | Display | ![]() |
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PDB format | ![]() | 246.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12888.555 Da / Num. of mol.: 1 / Fragment: RAS-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
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NMR experiment |
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Sample preparation
Sample conditions | pH: 6.5 / Temperature: 300 K |
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-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: DISTANCE GEOMETRY, ![]() | ||||||||||||||||
NMR ensemble | Conformer selection criteria: STRUCTURES WITH THE LOWEST TOTAL ENERGY AND NOE ENERGY WERE SELECTED Conformers calculated total number: 20 / Conformers submitted total number: 10 |