8hte

Crystal structure of an effector mutant in complex with ubiquitin

Method: X-RAY DIFFRACTION Dmax: 69.4 Å Quality: EXCELLENT

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

NAD(+)--protein-threonine ADP-ribosyltransferase

Chromobacterium violaceum ATCC 12472

UniProt Q7NY09

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 45–276 Mutation:E220A Ubiquitin × 1 (P0CH08) SO4 SULFATE ION × 2 GOL GLYCEROL × 2 NCA NICOTINAMIDE × 1 AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;100 mM BIS-TRIS propane, pH 7.0, and 1.5 M ammonium sulfate Resolution 2.31 Å R-free 0.228

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTEC_CHRVO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–233; UniProt 45–276

Ubiquitin

Saccharomyces cerevisiae S288C

UniProt P0CH08

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 1–76 Not recorded NAD(+)--protein-threonine ADP-ribosyltransferase × 1 (Q7NY09) SO4 SULFATE ION × 2 GOL GLYCEROL × 2 NCA NICOTINAMIDE × 1 AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;100 mM BIS-TRIS propane, pH 7.0, and 1.5 M ammonium sulfate Resolution 2.31 Å R-free 0.228

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.

179 other PDB entries and 217 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL40A_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–76; UniProt 1–76

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 8hte

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8hte
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8hte
Deposition date deposition_date2022-12-21
Structure title titleCrystal structure of an effector mutant in complex with ubiquitin
Keywords keywordsTransferase, Ubiquitination; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.70
Radius of gyration Rg (electron density) rg_electron20.72
Forward intensity I(0) i021198100.00
Molecular weight molecular_weight33870.0 kDa
Excluded volume excluded_volume41882 ų
Envelope volume envelope_volume50514 ų
Hydration-shell volume shell_volume20657 ų
Envelope diameter envelope_diameter69.6
Shell Rg shell_rg26.65
Envelope Rg envelope_rg20.67
Shape Rg shape_rg20.70
Total Rg total_rg21.55
Total atoms total_atoms2380
Residues n_residues297
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 dmax69.4
Rg (real space) rg_real21.65
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.1200e+07
I(0) uncertainty (real space) i0_real_error3.0350e+05
Rg (reciprocal space) rg_reciprocal21.66
I(0) (reciprocal space) i0_reciprocal21200000.0000
Solution quality estimate total_estimate0.9005
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5341000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)