Current Protein Identity:Q63767
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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 |
|---|---|---|---|---|---|---|---|
| 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 |