4qxc

Crystal structure of histone demethylase KDM2A-H3K36ME2 with NOG

Method: X-RAY DIFFRACTION Dmax: 100.1 Å Quality: EXCELLENT

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

Lysine-specific demethylase 2A

Mus musculus

UniProt F6YRW4

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 36–364 Chain B; UniProt 450–517 Fragment:UNP residues 36-364 Fragment:UNP residues 450-517 Histone H3.2 × 1 (P84228) OGA N-OXALYLGLYCINE × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;0.1 M CITRATE NA 18% PEG 3350, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.75 Å R-free 0.204
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 36–364 Chain D; UniProt 450–517 Fragment:UNP residues 36-364 Fragment:UNP residues 450-517 Histone H3.2 × 1 (P84228) OGA N-OXALYLGLYCINE × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;0.1 M CITRATE NA 18% PEG 3350, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.75 Å R-free 0.204

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F6YRW4_MOUSE
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–329; UniProt 36–364 Author chain C; PDBConstruct 1–329; UniProt 36–364 Author chain B; PDBConstruct 1–68; UniProt 450–517 Author chain D; PDBConstruct 1–68; UniProt 450–517

Histone H3.2

OrganismNot specified

UniProt P84228

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 E; UniProt 30–44 Fragment:UNP residues 30-44 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase 2A × 1 (F6YRW4) Lysine-specific demethylase 2A × 1 (F6YRW4) OGA N-OXALYLGLYCINE × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;0.1 M CITRATE NA 18% PEG 3350, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.75 Å R-free 0.204
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 30–44 Fragment:UNP residues 30-44 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase 2A × 1 (F6YRW4) Lysine-specific demethylase 2A × 1 (F6YRW4) OGA N-OXALYLGLYCINE × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;0.1 M CITRATE NA 18% PEG 3350, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.75 Å R-free 0.204

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.

7 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–15; UniProt 30–44 Author chain F; PDBConstruct 1–15; UniProt 30–44

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 4qxc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qxc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qxc
Deposition date deposition_date2014-07-19
Structure title titleCrystal structure of histone demethylase KDM2A-H3K36ME2 with NOG
Keywords keywordscupin subfamily Fe(II)/2-OG dioxygenase, JmjC domain, Histone demethylase, Oxidoreductase-Structural Protein complex; Oxidoreductase/Structural Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.38
Radius of gyration Rg (electron density) rg_electron30.33
Forward intensity I(0) i0140664000.00
Molecular weight molecular_weight95643.0 kDa
Excluded volume excluded_volume119930 ų
Envelope volume envelope_volume144920 ų
Hydration-shell volume shell_volume39418 ų
Envelope diameter envelope_diameter107.7
Shell Rg shell_rg37.92
Envelope Rg envelope_rg30.25
Shape Rg shape_rg30.26
Total Rg total_rg31.16
Total atoms total_atoms6727
Residues n_residues814
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 dmax100.1
Rg (real space) rg_real31.36
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.4070e+08
I(0) uncertainty (real space) i0_real_error2.0050e+06
Rg (reciprocal space) rg_reciprocal31.37
I(0) (reciprocal space) i0_reciprocal140700000.0000
Solution quality estimate total_estimate0.9015
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.0
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51350000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.925

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4qxcA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4qxcB00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology280 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily250
Domain ID domain_id4qxcC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4qxcD00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology280 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily250

8. Citations (1)

9. Files and Curves (10)