Current Protein Identity:P09055 New Search
Main Difference Dimensions in This Set
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
5XQ0 Structural basis of kindlin-mediated integrin recognition and activation Deposited 2017-06-05 Assembly 1 Insufficient information Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 784–798(15 aa) Fragment:UNP residues 784-798
Chain B 784–798(15 aa) Fragment:UNP residues 784-798
Mutation:168-217 deletion, 337-512 deletion Mutation:168-217 deletion, 337-512 deletion GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;0.2 M potassium chloride, 0.05 M HEPES pH 7.5, 35% v/v pentaerythritol propoxylate
Resolution 2.75 Å R-free 0.284
8TEC Crystal structure of Kindlin2 in complex with acylated beta1 integrin peptide Deposited 2023-07-06 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain C 784–798(15 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;0.1 M Tris, pH 8.5, 10% isopropanal
Resolution 2.04 Å R-free 0.230
8TEE Crystal structure of Kindlin2 in complex with K794Q mutated beta1 integrin Deposited 2023-07-06 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain C 784–798(15 aa)
Chain D 784–798(15 aa)
Mutation:K794Q Mutation:K794Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;298 K;0.1 M Tris, pH 8.5, 10% isopropanal
Resolution 2.49 Å R-free 0.275