9biv

Crystal Structure of Ubc13 with a New Active Site Loop Conformation

Method: X-RAY DIFFRACTION Dmax: 75.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ubiquitin-conjugating enzyme E2 variant 2

Homo sapiens

UniProt Q15819

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–145 Not recorded Ubiquitin-conjugating enzyme E2 N × 1 (P61088) X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 7.5;298 K;Ubc13-Mms2 heterodimer was concentrated to 12 mg/mL and stored in 50 mM Tris pH 7.5, 150 mM NaCl, 1mM TCEP. Complex was left to slowly equilibrate from 277K to 298 overnight Resolution 1.68 Å R-free 0.177

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.

17 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2V2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–145; UniProt 1–145

Ubiquitin-conjugating enzyme E2 N

Homo sapiens

UniProt P61088

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–152 Not recorded Ubiquitin-conjugating enzyme E2 variant 2 × 1 (Q15819) X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 7.5;298 K;Ubc13-Mms2 heterodimer was concentrated to 12 mg/mL and stored in 50 mM Tris pH 7.5, 150 mM NaCl, 1mM TCEP. Complex was left to slowly equilibrate from 277K to 298 overnight Resolution 1.68 Å R-free 0.177

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.

43 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2N_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–152; UniProt 1–152

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 9biv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9biv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9biv
Deposition date deposition_date2024-04-24
最后修订 last_revision2024-05-08
Structure title titleCrystal Structure of Ubc13 with a New Active Site Loop Conformation
Keywords keywordsE2, Conjugating, Enzyme, Ubiquitin, Ubc13, Mms2, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.51
Radius of gyration Rg (electron density) rg_electron22.55
Forward intensity I(0) i018373800.00
Molecular weight molecular_weight32605.0 kDa
Excluded volume excluded_volume40968 ų
Envelope volume envelope_volume50147 ų
Hydration-shell volume shell_volume19614 ų
Envelope diameter envelope_diameter79.1
Shell Rg shell_rg28.06
Envelope Rg envelope_rg22.57
Shape Rg shape_rg22.51
Total Rg total_rg23.42
Total atoms total_atoms4599
Residues n_residues288
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax75.8
Rg (real space) rg_real23.56
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.8370e+07
I(0) uncertainty (real space) i0_real_error2.5550e+05
Rg (reciprocal space) rg_reciprocal23.56
I(0) (reciprocal space) i0_reciprocal18370000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3410000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)