8k6v

LnaB-Actin-PRUb ternary complex

Method: X-RAY DIFFRACTION Dmax: 99.5 Å Quality: EXCELLENT

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

Actin gamma 1

OrganismNot specified

UniProt A0A8C6VAB1

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–375 Not recorded LnaB × 1 Ubiquitin × 1 (P0CG47) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 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:EVAPORATION;289 K;Magnesium acetate, MOPS, PEG8000 Resolution 2.60 Å R-free 0.307

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.

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

View Construct and Data Evidence
UniProt name A0A8C6VAB1_NAJNA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–375; UniProt 1–375

Ubiquitin

Homo sapiens

UniProt P0CG47

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–76 Not recorded Actin gamma 1 × 1 (A0A8C6VAB1) LnaB × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 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:EVAPORATION;289 K;Magnesium acetate, MOPS, PEG8000 Resolution 2.60 Å R-free 0.307

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; 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 8k6v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k6v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k6v
Deposition date deposition_date2023-07-25
Structure title titleLnaB-Actin-PRUb ternary complex
Keywords keywordsAMPylation, Legionella effector, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.61
Radius of gyration Rg (electron density) rg_electron31.02
Forward intensity I(0) i0127265000.00
Molecular weight molecular_weight89888.0 kDa
Excluded volume excluded_volume112560 ų
Envelope volume envelope_volume139980 ų
Hydration-shell volume shell_volume37655 ų
Envelope diameter envelope_diameter105.4
Shell Rg shell_rg37.98
Envelope Rg envelope_rg31.05
Shape Rg shape_rg31.03
Total Rg total_rg31.60
Total atoms total_atoms6352
Residues n_residues788
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 dmax99.5
Rg (real space) rg_real31.58
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real1.2730e+08
I(0) uncertainty (real space) i0_real_error1.9790e+06
Rg (reciprocal space) rg_reciprocal31.60
I(0) (reciprocal space) i0_reciprocal127300000.0000
Solution quality estimate total_estimate0.9056
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.585
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29340000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)