Brand  (β version)

  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
CAG Guanosine 5'-triphosphate p3-[1-(2-nitrophenyl)ethyl ester]
MG Magnesium ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1GNQ   PDBj   RCSB PDB   PDBe
Header : GTP BINDING PROTEIN
Title : X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP
Release Data : 1995-07-31
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 : Scheidig, A., Franken, S.M., Corrie, J.E.T., Reid, G.P., Wittinghofer, A., Pai, E.F., Goody, R.S.
Keywords : GTP BINDING PROTEIN
Exp. method : X-RAY DIFFRACTION ( 2.5 Å )
Citation :

X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp.

Scheidig, A.J.,Franken, S.M.,Corrie, J.E.  et al.
(1995)  J.Mol.Biol.  253 : 132 - 150

PubMed: 7473708
DOI: 10.1006/jmbi.1995.0541

Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points

Scheidig, A.J.,Sanchez-Llorente, A.,Lautwein, A.  et al.
(1994)  Acta Crystallogr.,Sect.D  50 : 512

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