4ip3

Complex structure of OspI and Ubc13

Method: X-RAY DIFFRACTION Dmax: 72.8 Å Quality: GOOD

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

ORF169b

Shigella flexneri

UniProt Q8VSD5

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 1–212 Mutation:C62A Ubiquitin-conjugating enzyme E2 N × 1 (P61088) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;0.2 M Sodium thiocyanate, 20% PEG3350, 0.1 M HEPES pH7.0, VAPOR DIFFUSION, temperature 298K Resolution 2.30 Å R-free 0.248

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.

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

View Construct and Data Evidence
UniProt name Q8VSD5_SHIFL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–214; UniProt 1–212

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 ORF169b × 1 (Q8VSD5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;0.2 M Sodium thiocyanate, 20% PEG3350, 0.1 M HEPES pH7.0, VAPOR DIFFUSION, temperature 298K Resolution 2.30 Å R-free 0.248

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 21–172; 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 4ip3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ip3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4ip3
Deposition date deposition_date2013-01-09
Structure title titleComplex structure of OspI and Ubc13
Keywords keywordsPapain fold, UNKNOWN FUNCTION-Ligase complex; UNKNOWN FUNCTION/Ligase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.79
Radius of gyration Rg (electron density) rg_electron21.75
Forward intensity I(0) i025529300.00
Molecular weight molecular_weight38224.0 kDa
Excluded volume excluded_volume47690 ų
Envelope volume envelope_volume57022 ų
Hydration-shell volume shell_volume22229 ų
Envelope diameter envelope_diameter75.1
Shell Rg shell_rg28.42
Envelope Rg envelope_rg21.99
Shape Rg shape_rg21.74
Total Rg total_rg22.62
Total atoms total_atoms2689
Residues n_residues343
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 dmax72.8
Rg (real space) rg_real22.79
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.5530e+07
I(0) uncertainty (real space) i0_real_error2.9050e+05
Rg (reciprocal space) rg_reciprocal22.79
I(0) (reciprocal space) i0_reciprocal25530000.0000
Solution quality estimate total_estimate0.8999
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5628000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4ip3b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id4ip3A00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily140
Domain ID domain_id4ip3B00
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)