Current Protein Identity:Q03386 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1LFD CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS Deposited 1998-04-29 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 778–864(87 aa) Fragment:RAS-INTERACTING DOMAIN, C-TERMINAL DOMAIN
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5;pH 6.5
Resolution 2.10 Å R-free 0.282
1LFD CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS Deposited 1998-04-29 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 778–864(87 aa) Fragment:RAS-INTERACTING DOMAIN, C-TERMINAL DOMAIN
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5;pH 6.5
Resolution 2.10 Å R-free 0.282
1LXD CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN Deposited 1997-03-05 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 694–864(171 aa) Fragment:C-TERMINAL DOMAIN WHICH BINDS TO ACTIVE RAS
Chain B 694–864(171 aa) Fragment:C-TERMINAL DOMAIN WHICH BINDS TO ACTIVE RAS
Mutation:N-TERMINAL GS INHERITED FROM THE LINKER SEQUENCE OF THE CLONING VECTOR Mutation:N-TERMINAL GS INHERITED FROM THE LINKER SEQUENCE OF THE CLONING VECTOR No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG 8000, 0.1 M TRIS PH 8.5, AND 0.2 M CALCIUM ACETATE.
Resolution 2.40 Å R-free 0.298