6u9q

Crystal Structure Analysis of DNA-BCL11A Znf domain complex

Method: X-RAY DIFFRACTION Dmax: 62.9 Å Quality: GOOD

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

B-cell lymphoma/leukemia 11A

Homo sapiens

UniProt Q9H165

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 730–835 Not recorded DNA5 × 1 DNA3 × 1 ZN ZINC ION × 3 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;NaMalate~8.0 Resolution 1.83 Å R-free 0.195

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.

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

View Construct and Data Evidence
UniProt name BC11A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–110; UniProt 730–835

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 6u9q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6u9q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6u9q
Deposition date deposition_date2019-09-09
Structure title titleCrystal Structure Analysis of DNA-BCL11A Znf domain complex
Keywords keywordsTranscription factor, DNA-binding, Zn finger, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.47
Radius of gyration Rg (electron density) rg_electron17.26
Forward intensity I(0) i010849300.00
Molecular weight molecular_weight18120.0 kDa
Excluded volume excluded_volume19836 ų
Envelope volume envelope_volume25922 ų
Hydration-shell volume shell_volume13451 ų
Envelope diameter envelope_diameter63.0
Shell Rg shell_rg22.08
Envelope Rg envelope_rg17.59
Shape Rg shape_rg17.25
Total Rg total_rg17.92
Total atoms total_atoms1220
Residues n_residues115
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 dmax62.9
Rg (real space) rg_real17.50
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.0850e+07
I(0) uncertainty (real space) i0_real_error1.3460e+05
Rg (reciprocal space) rg_reciprocal17.49
I(0) (reciprocal space) i0_reciprocal10850000.0000
Solution quality estimate total_estimate0.7684
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.3
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.163
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1393000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.712; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.850; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)