6ip4

Crystal structure of Arabidopsis thaliana JMJ13 catalytic domain in complex with NOG and an H3K27me3 peptide

Method: X-RAY DIFFRACTION Dmax: 83.0 Å Quality: GOOD

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

Arabidopsis JMJ13

Arabidopsis thaliana

UniProt F4KIX0

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 90–578 Fragment:UNP residues 90-578 Histone H3.2 × 1 (P59226) NI NICKEL (II) ION × 1 ZN ZINC ION × 2 OGA N-OXALYLGLYCINE × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1M MES, pH 6.5, 8% dioxane, and 1.6M ammonium sulfate Resolution 2.60 Å R-free 0.246

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 F4KIX0_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–490; UniProt 90–578

Histone H3.2

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 B; UniProt 25–36 Fragment:UNP residues 25-36 Non-standard monomer:Yes (specific site not provided by mmCIF) Arabidopsis JMJ13 × 1 (F4KIX0) NI NICKEL (II) ION × 1 ZN ZINC ION × 2 OGA N-OXALYLGLYCINE × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1M MES, pH 6.5, 8% dioxane, and 1.6M ammonium sulfate Resolution 2.60 Å R-free 0.246

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 H32_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 25–36

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 6ip4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ip4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ip4
Deposition date deposition_date2018-11-02
Structure title titleCrystal structure of Arabidopsis thaliana JMJ13 catalytic domain in complex with NOG and an H3K27me3 peptide
Keywords keywordshistone modification, flowering, epigenetics, 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_guinier25.46
Radius of gyration Rg (electron density) rg_electron24.36
Forward intensity I(0) i050767600.00
Molecular weight molecular_weight54882.0 kDa
Excluded volume excluded_volume68407 ų
Envelope volume envelope_volume82658 ų
Hydration-shell volume shell_volume28334 ų
Envelope diameter envelope_diameter85.9
Shell Rg shell_rg31.68
Envelope Rg envelope_rg24.61
Shape Rg shape_rg24.28
Total Rg total_rg25.43
Total atoms total_atoms3835
Residues n_residues478
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 dmax83.0
Rg (real space) rg_real25.41
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real5.0770e+07
I(0) uncertainty (real space) i0_real_error7.3790e+05
Rg (reciprocal space) rg_reciprocal25.42
I(0) (reciprocal space) i0_reciprocal50770000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13810000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6ip4A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin

8. Citations (1)

9. Files and Curves (10)