4tn7

Crystal structure of mouse KDM2A-H3K36ME-NO complex

Method: X-RAY DIFFRACTION Dmax: 109.1 Å Quality: GOOD

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

Lysine-specific demethylase 2A

Mus musculus

UniProt P59997

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 Peptide × 1 FE FE (III) ION × 1 NO NITRIC OXIDE × 1 SIN SUCCINIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;100 mM Li-citrate 18-30% PEG 3350 Resolution 2.20 Å R-free 0.279
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 Peptide × 1 FE FE (III) ION × 1 SIN SUCCINIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;100 mM Li-citrate 18-30% PEG 3350 Resolution 2.20 Å R-free 0.279

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM2A_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

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 4tn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4tn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4tn7
Deposition date deposition_date2014-06-03
Structure title titleCrystal structure of mouse KDM2A-H3K36ME-NO complex
Keywords keywordsOxidoreductase; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.33
Radius of gyration Rg (electron density) rg_electron32.66
Forward intensity I(0) i0138150000.00
Molecular weight molecular_weight95172.0 kDa
Excluded volume excluded_volume119410 ų
Envelope volume envelope_volume148300 ų
Hydration-shell volume shell_volume38181 ų
Envelope diameter envelope_diameter115.0
Shell Rg shell_rg38.94
Envelope Rg envelope_rg32.65
Shape Rg shape_rg32.60
Total Rg total_rg33.35
Total atoms total_atoms6701
Residues n_residues812
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 dmax109.1
Rg (real space) rg_real33.44
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real1.3810e+08
I(0) uncertainty (real space) i0_real_error2.0390e+06
Rg (reciprocal space) rg_reciprocal33.40
I(0) (reciprocal space) i0_reciprocal138100000.0000
Solution quality estimate total_estimate0.8806
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.355
Kurtosis Kurtosis kurtosis-0.584
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41920000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.930; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4tn7A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4tn7B00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology280 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily250
Domain ID domain_id4tn7C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4tn7D00
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)