9m4s

crystal structure of Arabidopsis thaliana ING2 PHD finger in complex with an H3K4me3 peptide

Method: X-RAY DIFFRACTION Dmax: 45.7 Å Quality: GOOD

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

PHD finger protein ING2

Arabidopsis thaliana

UniProt B3H615

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 189–262 Not recorded Histone H3.1 × 1 (P59226) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.1M NiCl2, 20% PEG2000 MME, and 0.1M Tris, pH 8.5 Resolution 1.60 Å R-free 0.225

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 ING2_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–74; UniProt 189–262

Histone H3.1

OrganismNot specified

UniProt P59226

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 P; UniProt 2–11 Non-standard monomer:Yes (specific site not provided by mmCIF) PHD finger protein ING2 × 1 (B3H615) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.1M NiCl2, 20% PEG2000 MME, and 0.1M Tris, pH 8.5 Resolution 1.60 Å R-free 0.225

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.

36 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–10; UniProt 2–11

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 9m4s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m4s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m4s
Deposition date deposition_date2025-03-04
最后修订 last_revision2025-11-05
Structure title titlecrystal structure of Arabidopsis thaliana ING2 PHD finger in complex with an H3K4me3 peptide
Keywords keywordshistone modification, epigenetic regulation, H3K4me3, ING1, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.01
Radius of gyration Rg (electron density) rg_electron12.02
Forward intensity I(0) i01644310.00
Molecular weight molecular_weight8104.0 kDa
Excluded volume excluded_volume9875 ų
Envelope volume envelope_volume11490 ų
Hydration-shell volume shell_volume8515 ų
Envelope diameter envelope_diameter45.5
Shell Rg shell_rg17.16
Envelope Rg envelope_rg12.70
Shape Rg shape_rg12.06
Total Rg total_rg13.20
Total atoms total_atoms558
Residues n_residues68
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 dmax45.7
Rg (real space) rg_real13.00
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.6440e+06
I(0) uncertainty (real space) i0_real_error1.8570e+04
Rg (reciprocal space) rg_reciprocal13.00
I(0) (reciprocal space) i0_reciprocal1644000.0000
Solution quality estimate total_estimate0.8579
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.1
Skewness Skewness skewness0.359
Kurtosis Kurtosis kurtosis-0.090
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha257500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.732; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)