Current Protein Identity:P68133 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
7RNS nSH2 domain of p85-alpha subunit of phosphatidylinositol 3-kinase in complex with an actin peptide with phosphorylated tyrosine 53 Deposited 2021-07-29 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 52–60(9 aa) Fragment:UNP residues 52-60
Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;292 K;0.05 M cadmium sulfate hydrate, 0.1 M HEPES, pH 7.5, 1.0 M sodium acetate trihydrate
Resolution 1.14 Å R-free 0.147
7RNU nSH2 domain of p85-beta subunit of phosphatidylinositol 3-kinase in complex with an actin peptide with phosphorylated tyrosine 53 Deposited 2021-07-29 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 52–60(9 aa) Fragment:UNP residues 52-60
Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5;292 K;25% w/v PEG1500, 100 mM MIB, pH 5.0
Resolution 1.45 Å R-free 0.222
7RNU nSH2 domain of p85-beta subunit of phosphatidylinositol 3-kinase in complex with an actin peptide with phosphorylated tyrosine 53 Deposited 2021-07-29 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 52–60(9 aa) Fragment:UNP residues 52-60
Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5;292 K;25% w/v PEG1500, 100 mM MIB, pH 5.0
Resolution 1.45 Å R-free 0.222
7RNU nSH2 domain of p85-beta subunit of phosphatidylinositol 3-kinase in complex with an actin peptide with phosphorylated tyrosine 53 Deposited 2021-07-29 Assembly 3 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain F 52–60(9 aa) Fragment:UNP residues 52-60
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, SITTING DROP;pH 5;292 K;25% w/v PEG1500, 100 mM MIB, pH 5.0
Resolution 1.45 Å R-free 0.222
7RNU nSH2 domain of p85-beta subunit of phosphatidylinositol 3-kinase in complex with an actin peptide with phosphorylated tyrosine 53 Deposited 2021-07-29 Assembly 4 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain H 52–60(9 aa) Fragment:UNP residues 52-60
Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5;292 K;25% w/v PEG1500, 100 mM MIB, pH 5.0
Resolution 1.45 Å R-free 0.222
7RNV SH2 domain of guanine nucleotide exchange factor Vav2 in complex with an actin peptide with phosphorylated tyrosine 53 Deposited 2021-07-29 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 52–60(9 aa) Fragment:UNP residues 52-60
Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.5;292 K;0.2 M sodium acetate trihydrate, 0.1 M Tris hydrochloride, pH 8.5, 30% PEG4000
Resolution 2.15 Å R-free 0.272
9DUU Cryo-EM structure of recombinant wildtype ACTA1 phalloidin-stabilized F-actin Deposited 2024-10-04 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 3–377(375 aa)
Chain B 3–377(375 aa)
Chain C 3–377(375 aa)
Chain D 3–377(375 aa)
Chain E 3–377(375 aa)
Chain F 3–377(375 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7;25 mM KCl, 2 mM EGTA, 60 mM MOPS (pH7), 1 mM DTT, and 4 mM MgCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9DUV Cryo-EM structure of recombinant R254H ACTA1 phalloidin-stabilized F-actin Deposited 2024-10-04 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 3–377(375 aa)
Chain B 3–377(375 aa)
Chain C 3–377(375 aa)
Chain D 3–377(375 aa)
Chain E 3–377(375 aa)
Chain F 3–377(375 aa)
Mutation:R254H Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:R254H Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:R254H Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:R254H Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:R254H Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:R254H Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7;25 mM KCl, 2 mM EGTA, 60 mM MOPS (pH7), 1 mM DTT, and 4 mM MgCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å