Current Protein Identity：Q60787
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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 |
|---|---|---|---|---|---|---|---|
| 1OEB Mona/Gads SH3C domain Deposited 2003-03-24 | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain D
231–243（13 aa）
Fragment：PROTEIN INTERACTION PEPTIDE, RESIDUES 231-243
|
Not recorded | CD CADMIUM ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 6.5；PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5
|
Resolution 1.76 Å R-free 0.235 |
| 1OEB Mona/Gads SH3C domain Deposited 2003-03-24 | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain C
231–243（13 aa）
Fragment：PROTEIN INTERACTION PEPTIDE, RESIDUES 231-243
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 6.5；PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5
|
Resolution 1.76 Å R-free 0.235 |
| 2ETZ The NMR minimized average structure of the Itk SH2 domain bound to a phosphopeptide Deposited 2005-10-27 | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain B
143–148（6 aa）
Fragment：phosphopeptide fragment sequence database residues 143-148
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 7.4；298 K；Ionic strength (raw mmCIF value) 125mM；Pressure ambient
NMR sample composition
1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90% H2O/10% D2O
NMR sample composition
U-15N labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90% H2O/10% D2O
NMR sample composition
U-15N, 13-C labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90%H20, 10%D2O
NMR sample composition
5mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90%H20, 10%D2O
NMR sample composition
1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 100% D2O
|
Resolution not provided |
| 2EU0 The NMR ensemble structure of the Itk SH2 domain bound to a phosphopeptide Deposited 2005-10-27 | Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain B
143–148（6 aa）
Fragment：phosphopeptide fragment, sequence database residues 143-148
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 7.4；298 K；Ionic strength (raw mmCIF value) 125mM；Pressure ambient
NMR sample composition
1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90% H2O/10% D2O
NMR sample composition
U-15N labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90% H2O/10% D2O
NMR sample composition
U-15N, 13-C labeled, 1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90% H2O/10% D2O
NMR sample composition
5mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 90%H20, 10%D2O
NMR sample composition
1mM Itk SH2 domain, 20mM phosphopeptide, 50mM KH2PO4, 75mM NaCl, 2mM DTT, 0.02% NaN3, pH 7.4 | 100% D2O
|
Resolution not provided |