Current Protein Identity:P35127
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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 |
|---|---|---|---|---|---|---|---|
| 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 |