Current Protein Identity:Q03386
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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 |