Current Protein Identity:Q15438 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different ligand/ion Different experimental method 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
1BC9 CYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-05-06 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 58–256(199 aa) Fragment:SEC7 DOMAIN,
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8;305 K;Ionic strength (raw mmCIF value) 0.47 M;Pressure 1
NMR sample composition 20 MM NAPI, 150 MM (NH4)2SO4, 3MM DTT, 10% D2O
Resolution not provided
4A4P crystal structure of the Sec7 domain from human cytohesin1 Deposited 2011-10-19 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 63–248(186 aa) Fragment:SEC7 DOMAIN, RESIDUES 63-248
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7;PEG 3350 12%, AMMONIUM ACETATE 0.4M. GLYCEROL CRYO-PROTECTANT., pH 7
Resolution 2.00 Å R-free 0.222
4A4P crystal structure of the Sec7 domain from human cytohesin1 Deposited 2011-10-19 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 63–248(186 aa) Fragment:SEC7 DOMAIN, RESIDUES 63-248
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7;PEG 3350 12%, AMMONIUM ACETATE 0.4M. GLYCEROL CRYO-PROTECTANT., pH 7
Resolution 2.00 Å R-free 0.222