4gu0

Crystal structure of LSD2 with H3

Method: X-RAY DIFFRACTION Dmax: 177.2 Å Quality: GOOD

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

Lysine-specific histone demethylase 1B

Homo sapiens

UniProt Q8NB78

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 51–822 Chain C; UniProt 51–822 Fragment:UNP residues 51-822 Histone H3.3 × 1 (P84243) FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.2M (NH4)2 Tartrate, 0.1M HEPES, 10% PEG20000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.10 Å R-free 0.221
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 51–822 Chain D; UniProt 51–822 Fragment:UNP residues 51-822 Histone H3.3 × 1 (P84243) FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.2M (NH4)2 Tartrate, 0.1M HEPES, 10% PEG20000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.10 Å R-free 0.221

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.

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

View Construct and Data Evidence
UniProt name KDM1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–776; UniProt 51–822 Author chain B; PDBConstruct 5–776; UniProt 51–822 Author chain C; PDBConstruct 5–776; UniProt 51–822 Author chain D; PDBConstruct 5–776; UniProt 51–822

Histone H3.3

OrganismNot specified

UniProt P84243

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 2–27 Fragment:UNP residues 2-27 Mutation:K4M Lysine-specific histone demethylase 1B × 2 (Q8NB78) FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.2M (NH4)2 Tartrate, 0.1M HEPES, 10% PEG20000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.10 Å R-free 0.221
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 2–27 Fragment:UNP residues 2-27 Mutation:K4M Lysine-specific histone demethylase 1B × 2 (Q8NB78) FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.2M (NH4)2 Tartrate, 0.1M HEPES, 10% PEG20000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.10 Å R-free 0.221

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.

94 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–26; UniProt 2–27 Author chain F; PDBConstruct 1–26; UniProt 2–27

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 4gu0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gu0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gu0
Deposition date deposition_date2012-08-29
Structure title titleCrystal structure of LSD2 with H3
Keywords keywordshistone demethylase, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier50.53
Radius of gyration Rg (electron density) rg_electron50.21
Forward intensity I(0) i01698790000.00
Molecular weight molecular_weight343530.0 kDa
Excluded volume excluded_volume429570 ų
Envelope volume envelope_volume577700 ų
Hydration-shell volume shell_volume95981 ų
Envelope diameter envelope_diameter197.0
Shell Rg shell_rg54.01
Envelope Rg envelope_rg49.69
Shape Rg shape_rg50.15
Total Rg total_rg50.56
Total atoms total_atoms24100
Residues n_residues3019
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 dmax177.2
Rg (real space) rg_real50.61
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real1.6990e+09
I(0) uncertainty (real space) i0_real_error3.2600e+07
Rg (reciprocal space) rg_reciprocal50.46
I(0) (reciprocal space) i0_reciprocal1698000000.0000
Solution quality estimate total_estimate0.8292
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.9
Skewness Skewness skewness0.506
Kurtosis Kurtosis kurtosis0.156
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha176500000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.661

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)