8gbq

Structure of RNF125 in complex with UbcH5b

Method: X-RAY DIFFRACTION Dmax: 71.5 Å Quality: REASONABLE

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

Ubiquitin-conjugating enzyme E2 D2

Homo sapiens

UniProt P62837

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 1–147 Not recorded E3 ubiquitin-protein ligase RNF125 × 1 (Q96EQ8) GOL GLYCEROL × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.5;289 K;0.1 M CHES 9.5 20% PEG 8000 Resolution 1.74 Å R-free 0.201

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.

57 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–152; UniProt 1–147

E3 ubiquitin-protein ligase RNF125

Homo sapiens

UniProt Q96EQ8

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 32–127 Not recorded Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) GOL GLYCEROL × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.5;289 K;0.1 M CHES 9.5 20% PEG 8000 Resolution 1.74 Å R-free 0.201

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.

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

View Construct and Data Evidence
UniProt name RN125_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–101; UniProt 32–127

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 8gbq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8gbq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8gbq
Deposition date deposition_date2023-02-27
Structure title titleStructure of RNF125 in complex with UbcH5b
Keywords keywordsubiquitin RING E3 ligase Ubiquitin conjugating enzyme Complex, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.83
Radius of gyration Rg (electron density) rg_electron21.01
Forward intensity I(0) i014120900.00
Molecular weight molecular_weight27720.0 kDa
Excluded volume excluded_volume34490 ų
Envelope volume envelope_volume41747 ų
Hydration-shell volume shell_volume17672 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg26.22
Envelope Rg envelope_rg21.01
Shape Rg shape_rg21.00
Total Rg total_rg21.80
Total atoms total_atoms1932
Residues n_residues240
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 dmax71.5
Rg (real space) rg_real21.90
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.4120e+07
I(0) uncertainty (real space) i0_real_error1.8920e+05
Rg (reciprocal space) rg_reciprocal21.89
I(0) (reciprocal space) i0_reciprocal14120000.0000
Solution quality estimate total_estimate0.6961
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2833000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 0.207; Positv: 1.000; Valcen: 0.899; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8gbqA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme

8. Citations (1)

9. Files and Curves (10)