Current Protein Identity:Q63767 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
1X27 Crystal Structure of Lck SH2-SH3 with SH2 binding site of p130Cas Deposited 2005-04-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain I 759–767(9 aa) Fragment:residues 759-767
Chain J 759–767(9 aa) Fragment:residues 759-767
Chain K 759–767(9 aa) Fragment:residues 759-767
Chain L 759–767(9 aa) Fragment:residues 759-767
Chain M 759–767(9 aa) Fragment:residues 759-767
Chain N 759–767(9 aa) Fragment:residues 759-767
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) NA SODIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;295 K;N-tris[hydroxymethyl]methyl-3-aminopropane-sulfonic acid, di_potasium hydrogen phosphate, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.70 Å R-free 0.317
1Z23 The serine-rich domain from Crk-associated substrate (p130Cas) Deposited 2005-03-07 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 546–708(163 aa) Fragment:serine-rich domain, SRR-B, residues 546-708
Mutation:V546G P547S No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.9;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient
NMR sample composition 1.8mM protein U-15N, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O; | 90% H2O/10% D2O
NMR sample composition 1.8mM protein U-13C, U-15N, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1.8mM protein U-13C, U-15N, ~60% 2H, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1.8mM protein U-15N, ~60% 2H, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided