8sr6

Crystal structure of legAS4 from Legionella pneumophila subsp. pneumophila with histone H3 (3-17)peptide

Method: X-RAY DIFFRACTION Dmax: 80.9 Å Quality: EXCELLENT

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

Eukaryotic huntingtin interacting protein B

Legionella pneumophila subsp. pneumophila

UniProt Q5ZUS4

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 84–532 Not recorded SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 10 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.1M Bis-Tris 6.5 and 38% PPG P400 Resolution 2.22 Å R-free 0.230

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5ZUS4_LEGPH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–451; UniProt 84–532

Histone 3 peptide

OrganismNot specified

UniProt Q6NXT2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 4–18 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.1M Bis-Tris 6.5 and 38% PPG P400 Resolution 2.22 Å R-free 0.230

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.

22 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 4–18

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 8sr6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sr6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8sr6
Deposition date deposition_date2023-05-05
Structure title titleCrystal structure of legAS4 from Legionella pneumophila subsp. pneumophila with histone H3 (3-17)peptide
Keywords keywordsankyrin repeats, histone methyltransferase activity, CELL INVASION; CELL INVASION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.42
Radius of gyration Rg (electron density) rg_electron24.48
Forward intensity I(0) i049173300.00
Molecular weight molecular_weight54231.0 kDa
Excluded volume excluded_volume67751 ų
Envelope volume envelope_volume81852 ų
Hydration-shell volume shell_volume27837 ų
Envelope diameter envelope_diameter85.5
Shell Rg shell_rg31.81
Envelope Rg envelope_rg24.81
Shape Rg shape_rg24.46
Total Rg total_rg25.38
Total atoms total_atoms3824
Residues n_residues466
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 dmax80.9
Rg (real space) rg_real25.36
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real4.9170e+07
I(0) uncertainty (real space) i0_real_error7.0550e+05
Rg (reciprocal space) rg_reciprocal25.38
I(0) (reciprocal space) i0_reciprocal49170000.0000
Solution quality estimate total_estimate0.9055
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12630000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)