Current Protein Identity:P61864 New Search
Main Difference Dimensions in This Set
Different mutation/modification Different assembly state Different ligand/ion 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
1OTR Solution Structure of a CUE-Ubiquitin Complex Deposited 2003-03-22 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7;298 K;Ionic strength (raw mmCIF value) 20 mM sodium phosphate, pH 7.0, 0.2% NaN3;Pressure 1
NMR sample composition 1 mM U-15N,13C Cue2 + 1 mM Ubiquitin; 20 mM sodium phosphate buffer, pH 7.0, 0.2% NaN3 | 90% H2O/10% D2O
NMR sample composition 1 mM U-15N,13C Cue2 + 1 mM Ubiquitin; 20 mM sodium phosphate buffer, pH 7.0, 0.2% NaN3 | 99.996% D2O
NMR sample composition 1 mM Cue2 + 1 mM U-15N,13C Ubiquitin; 20 mM sodium phosphate buffer, pH 7.0, 0.2% NaN3 | 90% H2O/10% D2O
NMR sample composition 1 mM Cue2 + 1 mM U-15N,13C Ubiquitin; 20 mM sodium phosphate buffer, pH 7.0, 0.2% NaN3 | 99.996% D2O
Resolution not provided
1Q0W Solution structure of Vps27 amino-terminal UIM-ubiquitin complex Deposited 2003-07-17 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;298 K;Ionic strength (raw mmCIF value) 20 mM sodium phosphate, pH 6.0, 0.2% NaN3;Pressure 1
NMR sample composition 1 mM U-15N,13C Ubiquitin + 1 mM Vps27 amino-terminal UIM | 90% H2O/10% D2O
NMR sample composition 1 mM U-15N,13C Ubiquitin + 1 mM Vps27 amino-terminal UIM | 100% D2O
Resolution not provided
1WR1 The complex structure of Dsk2p UBA with ubiquitin Deposited 2004-10-08 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–76(76 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8;298 K;Ionic strength (raw mmCIF value) 20mM potassium phosphate, 5mM potassium chloride
NMR sample composition U-15N, 13C ubiquitin + DSK2-UBA complex (0.9mM) | 20mM Phosphate buffer (pH 6.8); 5mM potassium chloride; 1mM EDTA; 5% D2O
NMR sample composition U-15N, 13C DSK2-UBA + ubiquitin complex (1.0mM) | 20mM Phosphate buffer (pH 6.8); 5mM potassium chloride; 1mM EDTA; 5% D2O
Resolution not provided
1ZGU Solution structure of the human Mms2-Ubiquitin complex Deposited 2005-04-22 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa)
Mutation:K48R No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5;293 K;Ionic strength (raw mmCIF value) 150 mM NaCl;Pressure 1
NMR measurement conditions pH 7.5;303 K;Ionic strength (raw mmCIF value) 150 mM NaCl;Pressure 1
NMR sample composition [U-15N; U-10% 13C]-hMms2 + Ubiquitin (1:4 ratio) 90% H20 : 10% D20 | 90% H20 : 10% D20
NMR sample composition [U-13C; U-15N]-Ubiquitin + hMms2 (4:1 ratio) 90% H20 : 10% D20 | 90% H20 : 10% D20
NMR sample composition [U-13C; U-15N]-hMms2 + Ubiquitin (1:4 ratio) 90% H20 : 10% D20 | 90% H20 : 10% D20
Resolution not provided
1ZW7 Elimination of the C-cap in Ubiquitin Structure, Dynamics and Thermodynamic Consequences Deposited 2005-06-03 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–76(76 aa)
Mutation:R42E, E34P No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5;298 K;Ionic strength (raw mmCIF value) 30 mM actate;Pressure Ambient
NMR sample composition 1-2 mM of appropriately labeled mutant ubiquitin | 30 mM acetate buffer, pH 5.0
Resolution not provided
2G3Q Solution Structure of Ede1 UBA-ubiquitin complex Deposited 2006-02-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;298 K;Ionic strength (raw mmCIF value) 20mM Sodium Phosphate;Pressure 1
NMR sample composition 1mM 15N,13C-labeled Ede1 UBA; 1mM Ubiquitin; 20mM phosphate buffer (pH 6.0), 2mM DTT, 0.2% NaN3, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM 15N,13C-labeled Ede1 UBA; 1mM Ubiquitin; 20mM phosphate buffer (pH 6.0), 2mM DTT, 0.2% NaN3, 100% D2O | 100% D2O
NMR sample composition 1mM Ede1 UBA; 1mM 15N,13C-labeled Ubiquitin; 20mM phosphate buffer (pH 6.0), 2mM DTT, 0.2% NaN3, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM Ede1 UBA; 1mM 15N,13C-labeled Ubiquitin; 20mM phosphate buffer (pH 6.0), 2mM DTT, 0.2% NaN3, 100% D2O | 100% D2O
Resolution not provided
2JT4 Solution Structure of the Sla1 SH3-3-Ubiquitin Complex Deposited 2007-07-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa) Fragment:SH3 domain sequence database residues 350-420
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;318 K;Ionic strength (raw mmCIF value) 20;Pressure ambient
NMR sample composition 0.9 mM [U-98% 13C; U-98% 15N] SH3, 0.9 mM ubiquitin, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.9 mM [U-98% 13C; U-98% 15N] ubiquitin, 0.9 mM SH3, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.9 mM [U-98% 13C; U-98% 15N] SH3, 0.9 mM ubiquitin, 100% D2O | 100% D2O
NMR sample composition 0.9 mM [U-98% 13C; U-98% 15N] ubiquitin, 0.9 mM SH3, 100% D2O | 100% D2O
Resolution not provided
2JWZ Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins Deposited 2007-10-31 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–76(76 aa)
Mutation:L69S No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8;296 K;Ionic strength (raw mmCIF value) 20 mM;Pressure AMBIENT
NMR sample composition 2 mM [U-100% 15N] L69S UBIQUITIN, 2 mM L69S UBIQUITIN, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
2L00 Solution structure of the non-covalent complex of the ZNF216 A20 domain with ubiquitin Deposited 2010-06-29 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa) Fragment:ubiquitin core domain
Not recorded ZN ZINC ION × 1 SOLUTION NMR
NMR measurement conditions pH 7;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient
NMR sample composition 4 mM ZNF216-A20-1, 50 uM Zinc-2, 0.1 mM DSS-3, 5 mM TRIS-4, 50 mM sodium chloride-5, 1 mM [U-100% 15N] ubiquitin-6, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM [U-100% 15N] ZNF216-A20-7, 50 uM Zinc-8, 4 mM MTSL-9, 5 mM TRIS-10, 50 mM sodium chloride-11, 4 mM ubiquitin-12, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.8 mM [U-100% 13C; U-100% 15N] ZNF216-A20-13, 50 uM Zinc-14, 0.1 mM DSS-15, 5 mM TRIS-16, 50 mM sodium chloride-17, 2 mM ubiquitin-18, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM [U-100% 15N] ZNF216-A20-19, 50 uM Zinc-20, 0.1 mM DSS-21, 5 mM TRIS-22, 50 mM sodium chloride-23, 5 % Polyacrylamide gel-24, 4 mM ubiquitin-25, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 4 mM ZNF216-A20-26, 50 uM Zinc-27, 0.1 mM DSS-28, 5 mM TRIS-29, 50 mM sodium chloride-30, 5 % Polyacrylamide gel-31, 1 mM [U-100% 15N] ubiquitin-32, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2 mM ZNF216-A20-33, 50 uM Zinc-34, 0.1 mM DSS-35, 5 mM TRIS-36, 50 mM sodium chloride-37, 1 mM [U-100% 13C; U-100% 15N] ubiquitin-38, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-100% 15N] ZNF216-A20-39, 50 uM Zinc-40, 0.1 mM DSS-41, 5 mM TRIS-42, 50 mM sodium chloride-43, 4 mM ubiquitin-44, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3CMM Crystal Structure of the Uba1-Ubiquitin Complex Deposited 2008-03-23 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa)
Not recorded PRO PROLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.6;298 K;L-proline, PEG 5000 MME, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.70 Å R-free 0.247
3CMM Crystal Structure of the Uba1-Ubiquitin Complex Deposited 2008-03-23 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 1–76(76 aa)
Not recorded PRO PROLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.6;298 K;L-proline, PEG 5000 MME, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.70 Å R-free 0.247
3L0W Structure of split monoubiquitinated PCNA with ubiquitin in position two Deposited 2009-12-10 Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa) Fragment:ubi-C fragment
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;291 K;2.04 M ammonium sulfate, 0.1 M sodium citrate, 3% ethanol, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.314
3L10 Structure of split monoubiquitinated PCNA with ubiquitin in position one Deposited 2009-12-10 Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa) Fragment:Ubi-C fragment
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;291 K;2.04M ammonium sulfate, 0.1M sodium citrate, 3% ethanol, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.314