Current Protein Identity:P0CG53 New Search
Main Difference Dimensions in This Set
Different construct 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
1E0Q Mutant Peptide from the first N-terminal 17 amino-acid of Ubiquitin Deposited 2000-04-05 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–17(17 aa) Fragment:RESIDUES 1-17
Mutation:YES No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.8;275 K
NMR sample composition 10% WATER/90% D2O AND 90% WATER/10% D2O
Resolution not provided
2XBB Nedd4 HECT:Ub complex Deposited 2010-04-08 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 1–76(76 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;100 MM NA-HEPES, PH 7.5, 10% PEG 2000 MME, 5 MM TCEP.
Resolution 2.68 Å R-free 0.249
2XBB Nedd4 HECT:Ub complex Deposited 2010-04-08 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 1–76(76 aa)
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;100 MM NA-HEPES, PH 7.5, 10% PEG 2000 MME, 5 MM TCEP.
Resolution 2.68 Å R-free 0.249
4BBN NEDD4 HECT-Ub:Ub complex Deposited 2012-09-27 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain C 1–76(76 aa) Fragment:RESIDUES 1-76
Chain F 229–304(76 aa) Fragment:RESIDUES 229-304
Mutation:YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6;2.5 SODIUM MALONATE, PH 6.0
Resolution 2.51 Å R-free 0.224
5TR4 Structure of Ubiquitin activating enzyme (Uba1) in complex with ubiquitin and TAK-243 Deposited 2016-10-25 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–76(76 aa)
Not recorded 61T [(1~{R},2~{R},3~{S},4~{R})-2,3-bis(oxidanyl)-4-[[2-[3-(trifluoromethylsulfanyl)phenyl]pyrazolo[1,5-a]pyrimidin-7-yl]amino]cyclopentyl]methyl sulfamate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;70 mM Na malonate pH 6.0, 70 mM malic acid, 70 mM Na citrate, 10-15% peg-3350
Resolution 2.20 Å R-free 0.256
5TR4 Structure of Ubiquitin activating enzyme (Uba1) in complex with ubiquitin and TAK-243 Deposited 2016-10-25 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 1–76(76 aa)
Not recorded 61T [(1~{R},2~{R},3~{S},4~{R})-2,3-bis(oxidanyl)-4-[[2-[3-(trifluoromethylsulfanyl)phenyl]pyrazolo[1,5-a]pyrimidin-7-yl]amino]cyclopentyl]methyl sulfamate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;70 mM Na malonate pH 6.0, 70 mM malic acid, 70 mM Na citrate, 10-15% peg-3350
Resolution 2.20 Å R-free 0.256