Brand  (β version)

PDB ID: 1AGP

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
GNP Phosphoaminophosphonic acid-guanylate ester PoSSuM
MG Magnesium ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1AGP   PDBj   RCSB PDB   PDBe
Header : ONCOGENE PROTEIN
Title : THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLY-12 MUTANT OF P21-H-RAS
Release Data : 1994-04-30
Compound :
mol_id molecule chains
1 C-H-RAS P21 PROTEIN A
mutation: G12D
Source :
mol_id organism_scientific organism_common
1 Homo sapiens  (taxid:9606) Human
Authors : Franken, S.M., Scheidig, A.J., Wittinghofer, A., Goody, R.S.
Keywords : ONCOGENE PROTEIN
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras.

Franken, S.M.,Scheidig, A.J.,Krengel, U.  et al.
(1993)  Biochemistry  32 : 8411 - 8420

PubMed: 8357792
DOI: 10.1021/bi00084a005

Three-Dimensional Structures of H-Ras P21 Mutants: Molecular Basis for Their Inability to Function as Signal Switch Molecules

Krengel, U.,Schlichting, I.,Scherer, A.  et al.
(1990)  Cell(Cambridge,Mass.)  62 : 539

Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications for the Mechanism of GTP Hydrolysis

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

Reaction

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