Current Protein Identity:Q8X2D5 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different experimental conditions

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
2K42 Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector Deposited 2008-05-27 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 268–300(33 aa) Fragment:UNP residues 268-300
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8;298.15 K;Pressure ambient
NMR sample composition 1~1.5 mM [U-100% 13C; U-100% 15N] GBD/R33 complex, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1~1.5 mM [U-100% 13C; U-100% 15N] GBD/R33 complex, 100% D2O | 100% D2O
Resolution not provided
2KXC 1H, 13C, and 15N Chemical Shift Assignments for IRTKS-SH3 and EspFu-R47 complex Deposited 2010-04-30 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 268–314(47 aa) Fragment:EspFu-R47 domain, UNP residues 268-314
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7;298 K;Ionic strength (raw mmCIF value) 50;Pressure AMBIENT
NMR sample composition 0.48 mM [U-98% 13C; U-98% 15N] IRTKS-SH3-1, 0.48 mM EspFu-R47-2, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.9 mM [U-98% 13C; U-98% 15N] EspFu-R47-3, 0.9 mM IRTKS-SH3-4, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided