Current Protein Identity:P35127 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
1CMX STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES Deposited 1999-05-12 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–235(235 aa) Fragment:ALL
Chain C 1–235(235 aa) Fragment:ALL
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5;16% PEG 6000 0.1 M SODIUM ACETATE PH 4.4, pH 4.5
Resolution 2.25 Å R-free 0.285
7EN4 Multi-state structure determination and dynamics analysis elucidate a new ubiquitin-recognition mechanism of yeast ubiquitin C-terminal hydrolase. Deposited 2021-04-15 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–236(236 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;303 K;Ionic strength (raw mmCIF value) 100;Pressure AMBIENT
NMR sample composition 2 mM [U-100% 13C; U-100% 15N; U-50% 2H] ubiquitin hydrolase, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2 mM [U-100% 15N] ubiquitin hydrolase, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2 mM Ile/Leu/Val-methyl-selectively 1H/13C-labeled and Phe/Tyr/Trp-aromatic ring-selectively 1H-labeled ubiquitin hydrolase, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided