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- PDB-1gnp: X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE O... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gnp | ||||||
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Title | X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP | ||||||
![]() | C-H-RAS P21 PROTEIN | ||||||
![]() | GTP BINDING PROTEIN | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Scheidig, A. / Franken, S.M. / Corrie, J.E.T. / Reid, G.P. / Wittinghofer, A. / Pai, E.F. / Goody, R.S. | ||||||
![]() | ![]() Title: X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp. Authors: Scheidig, A.J. / Franken, S.M. / Corrie, J.E. / Reid, G.P. / Wittinghofer, A. / Pai, E.F. / Goody, R.S. #1: ![]() Title: Crystallographic Studies on P21H-Ras Using the Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points Authors: Scheidig, A.X. / Sanchez-Llorente, A. / Lautwein, A. / Pai, E.F. / Corrie, J.E.T. / Reid, G.P. / Wittinghofer, A. / Goody, R.S. #2: ![]() Title: Studies on the Structure and Mechanism of H-Ras P21 Authors: Goody, R.S. / Pai, E.F. / Schlichting, I. / Rensland, H. / Scheidig, A. / Franken, S.M. / Wittinghofer, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 46.1 KB | Display | ![]() |
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PDB format | ![]() | 31.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: GLU 62 - GLU 63 OMEGA = 144.55 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 18875.191 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-AGN / |
Compound details | SECONDARY STRUCTURE ELEMENTS HAVE BEEN ASSIGNED ACCORDING TO THE PROGRAM DSSP (KABSCH, W. & SANDER, ...SECONDARY STRUCTURE ELEMENTS HAVE BEEN ASSIGNED ACCORDING TO THE PROGRAM DSSP (KABSCH, W. & SANDER, C. (1983) BIOPOLYMER |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 37.48 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 7.6 / Method: batch method | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1992 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.6→30 Å / Num. obs: 5007 / % possible obs: 88.8 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Rmerge(I) obs: 0.075 |
Reflection | *PLUS Highest resolution: 2.6 Å / Num. measured all: 15930 / Rmerge(I) obs: 0.098 |
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Processing
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Refinement | Resolution: 2.7→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 11.72 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.44 |