8st9

Structure of E3 ligase NleL bound to ubiquitin

Method: X-RAY DIFFRACTION Dmax: 77.4 Å Quality: EXCELLENT

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

E3 ubiquitin-protein ligase SopA

Escherichia coli O157:H7 str. Sakai

UniProt A0A0H3JDV8

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 606–782 Not recorded Ubiquitin × 1 (P0CG48) AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;20% PEG 3350, 0.2 M KSCN, 0.1 M bis-tris propane pH 7.5, 20% glycerol, and 10% ethylene glycol Resolution 2.50 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 606–782 Not recorded Ubiquitin × 1 (P0CG48) AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;20% PEG 3350, 0.2 M KSCN, 0.1 M bis-tris propane pH 7.5, 20% glycerol, and 10% ethylene glycol Resolution 2.50 Å R-free 0.252

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0H3JDV8_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–179; UniProt 606–782 Author chain C; PDBConstruct 3–179; UniProt 606–782

Ubiquitin

Homo sapiens

UniProt P0CG48

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 1–75 Not recorded E3 ubiquitin-protein ligase SopA × 1 (A0A0H3JDV8) AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;20% PEG 3350, 0.2 M KSCN, 0.1 M bis-tris propane pH 7.5, 20% glycerol, and 10% ethylene glycol Resolution 2.50 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–75 Not recorded E3 ubiquitin-protein ligase SopA × 1 (A0A0H3JDV8) AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;20% PEG 3350, 0.2 M KSCN, 0.1 M bis-tris propane pH 7.5, 20% glycerol, and 10% ethylene glycol Resolution 2.50 Å R-free 0.252

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.

219 other PDB entries and 347 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–75; UniProt 1–75 Author chain D; PDBConstruct 1–75; UniProt 1–75

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 8st9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8st9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8st9
Deposition date deposition_date2023-05-09
Structure title titleStructure of E3 ligase NleL bound to ubiquitin
Keywords keywordsE3 ubiquitin ligase, LIGASE, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.01
Radius of gyration Rg (electron density) rg_electron24.92
Forward intensity I(0) i053570000.00
Molecular weight molecular_weight57729.0 kDa
Excluded volume excluded_volume72601 ų
Envelope volume envelope_volume86530 ų
Hydration-shell volume shell_volume28768 ų
Envelope diameter envelope_diameter81.1
Shell Rg shell_rg32.13
Envelope Rg envelope_rg24.78
Shape Rg shape_rg24.93
Total Rg total_rg25.71
Total atoms total_atoms4063
Residues n_residues505
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 dmax77.4
Rg (real space) rg_real25.88
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real5.3570e+07
I(0) uncertainty (real space) i0_real_error7.6470e+05
Rg (reciprocal space) rg_reciprocal25.93
I(0) (reciprocal space) i0_reciprocal53570000.0000
Solution quality estimate total_estimate0.9166
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.1
Skewness Skewness skewness0.097
Kurtosis Kurtosis kurtosis-0.689
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13650000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8st9A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology4140 — effector protein (NleL) fold
Homologous superfamily homologous superfamily10 — effector protein (NleL)
Domain ID domain_id8st9B01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id8st9C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology4140 — effector protein (NleL) fold
Homologous superfamily homologous superfamily10 — effector protein (NleL)
Domain ID domain_id8st9D01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (2)

9. Files and Curves (10)