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Ligands
Code Name Style Show Link
GNP Phosphoaminophosphonic acid-guanylate ester
MG Magnesium ion
Non-standard Residues
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Glycosylation
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Code : 5P21   PDBj   RCSB PDB   PDBe
Header : ONCOGENE PROTEIN
Title : REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS
Release Data : 1992-01-15
Compound :
mol_id molecule chains
1 C-H-RAS P21 PROTEIN A
Source :
mol_id organism_scientific organism_common
1 Homo sapiens  (taxid:9606) Human
Authors : Pai, E.F., Wittinghofer, A., Kabsch, W.
Keywords : ONCOGENE PROTEIN
Exp. method : X-RAY DIFFRACTION ( 1.35 Å )
Citation :

Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.

Pai, E.F.,Krengel, U.,Petsko, G.A.  et al.
(1990)  EMBO J.  9 : 2351 - 2359

PubMed: 2196171

Time-Resolved X-Ray Crystallographic Study of the Conformational Change in Ha-Ras P21 Protein on GTP Hydrolysis

Schlichting, I.,Almo, S.C.,Rapp, G.  et al.
(1990)  Nature  345 : 309

Crystallization and Preliminary X-Ray Analysis of the Human C-H-Ras-Oncogene Product P21 Complexed with GTP Analogues

Scherer, A.,John, J.,Linke, R.  et al.
(1989)  J.Mol.Biol.  206 : 257

Structure of the Guanine-Nucleotide-Binding Domain of the Ha-Ras Oncogene Product P21 in the Triphosphate Conformation

Pai, E.F.,Kabsch, W.,Krengel, U.  et al.
(1989)  Nature  341 : 209

Biochemical and Crystallographic Characterization of a Complex of C-Ha-Ras P21 and Caged GTP with Flash Photolysis

Schlichting, I.,Rapp, G.,John, J.  et al.
(1989)  Proc.Natl.Acad.Sci.USA  86 : 7687

Chain : A
UniProt : P01112 (RASH_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
GTP + H2O = GDP + phosphate + H(+) 3.6.5.2 PubMed:9020151
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