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1e0q

Mutant Peptide from the first N-terminal 17 amino-acid of Ubiquitin

Method: SOLUTION NMR Dmax: 34.7 Å Quality: SUSPICIOUS
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1. Protein Identity and Related Structures Protein Identity & Related Structures

POLYUBIQUITIN-B

OrganismNot specified

UniProt P0CG53

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–17 Fragment：RESIDUES 1-17 Mutation：YES No other associated polymer 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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1E0Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2XBB Nedd4 HECT:Ub complex Deposited 2010-04-08 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
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

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_BOVIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–17； UniProt 1–17

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1e0q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e0q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e0q
Deposition date deposition_date2000-04-05
Structure title titleMutant Peptide from the first N-terminal 17 amino-acid of Ubiquitin
Keywords keywordsPROTEIN BINDING, MUTANT PEPTIDE; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier9.05 Å
Radius of gyration Rg (electron density) rg_electron9.36 Å
Forward intensity I(0) i030182500.00
Molecular weight molecular_weight52281.0 kDa
Excluded volume excluded_volume68275 ų
Envelope volume envelope_volume4987 ų
Hydration-shell volume shell_volume4901 ų
Envelope diameter envelope_diameter34.6 Å
Shell Rg shell_rg14.24 Å
Envelope Rg envelope_rg10.60 Å
Shape Rg shape_rg9.26 Å
Total Rg total_rg9.95 Å
Total atoms total_atoms7695
Residues n_residues459
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax34.7 Å
Rg (real space) rg_real9.32 Å
Rg uncertainty (real space) rg_real_error0.40 Å
I(0) (real space) i0_real3.0180e+07
I(0) uncertainty (real space) i0_real_error3.2270e+05
Rg (reciprocal space) rg_reciprocal9.31 Å
I(0) (reciprocal space) i0_reciprocal30180000.0000
Solution quality estimate total_estimate0.4851
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary6.2 Å
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis-0.788
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1488.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.100; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.002; Smooth: 0.896
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1e0qa_
Class classj — Peptides
Fold Fold foldj.76 — Ubiquitin fragments
Superfamily Superfamily superfamilyj.76.1 — Ubiquitin fragments
Family Family familyj.76.1.1 — Ubiquitin fragments
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8. Citations (1)

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9. Files and Curves (10)