7e7a

Crystal structure of apo ENL YEATS domain T3 mutant

Method: X-RAY DIFFRACTION Dmax: 91.3 Å Quality: EXCELLENT

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

Protein ENL

Homo sapiens

UniProt Q03111

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–148 Mutation:N111K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;2M sodium formate, 0.1M sodium acetate trihydrate pH 4.6 Resolution 2.64 Å R-free 0.230
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–148 Mutation:N111K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;2M sodium formate, 0.1M sodium acetate trihydrate pH 4.6 Resolution 2.64 Å R-free 0.230
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–148 Mutation:N111K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;2M sodium formate, 0.1M sodium acetate trihydrate pH 4.6 Resolution 2.64 Å R-free 0.230
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–148 Mutation:N111K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;2M sodium formate, 0.1M sodium acetate trihydrate pH 4.6 Resolution 2.64 Å R-free 0.230

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.

25 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–149; UniProt 1–148 Author chain B; PDBConstruct 4–149; UniProt 1–148 Author chain C; PDBConstruct 4–149; UniProt 1–148 Author chain D; PDBConstruct 4–149; UniProt 1–148

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 7e7a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7e7a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7e7a
Deposition date deposition_date2021-02-25
Structure title titleCrystal structure of apo ENL YEATS domain T3 mutant
Keywords keywordsYEATS domain, Complex, histone, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.21
Radius of gyration Rg (electron density) rg_electron28.27
Forward intensity I(0) i066476900.00
Molecular weight molecular_weight65074.0 kDa
Excluded volume excluded_volume82106 ų
Envelope volume envelope_volume104530 ų
Hydration-shell volume shell_volume31435 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg34.91
Envelope Rg envelope_rg28.11
Shape Rg shape_rg28.19
Total Rg total_rg29.26
Total atoms total_atoms4584
Residues n_residues550
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 dmax91.3
Rg (real space) rg_real29.20
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real6.6480e+07
I(0) uncertainty (real space) i0_real_error8.8320e+05
Rg (reciprocal space) rg_reciprocal29.21
I(0) (reciprocal space) i0_reciprocal66480000.0000
Solution quality estimate total_estimate0.9035
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9833000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)