9b4p

Tetramer Formation of the BCL11A ZF0 Domain

Method: X-RAY DIFFRACTION Dmax: 74.6 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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 45–71 Chain C; UniProt 45–71 Fragment:ZF0 domain ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.3;291.15 K;0.2M potassium nitrate, 0.1M Tris-HCl pH 7.3, 20% PEG3350 Resolution 2.56 Å R-free 0.294
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 45–71 Chain D; UniProt 45–71 Chain E; UniProt 45–71 Chain F; UniProt 45–71 Fragment:ZF0 domain ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.3;291.15 K;0.2M potassium nitrate, 0.1M Tris-HCl pH 7.3, 20% PEG3350 Resolution 2.56 Å R-free 0.294
3 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 45–71 Chain H; UniProt 45–71 Chain I; UniProt 45–71 Chain J; UniProt 45–71 Fragment:ZF0 domain ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.3;291.15 K;0.2M potassium nitrate, 0.1M Tris-HCl pH 7.3, 20% PEG3350 Resolution 2.56 Å R-free 0.294

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 23 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 2–28; UniProt 45–71 Author chain B; PDBConstruct 2–28; UniProt 45–71 Author chain C; PDBConstruct 2–28; UniProt 45–71 Author chain D; PDBConstruct 2–28; UniProt 45–71 Author chain E; PDBConstruct 2–28; UniProt 45–71 Author chain F; PDBConstruct 2–28; UniProt 45–71 Author chain G; PDBConstruct 2–28; UniProt 45–71 Author chain H; PDBConstruct 2–28; UniProt 45–71 Author chain I; PDBConstruct 2–28; UniProt 45–71 Author chain J; PDBConstruct 2–28; UniProt 45–71

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 9b4p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b4p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b4p
Deposition date deposition_date2024-03-21
最后修订 last_revision2024-12-18
Structure title titleTetramer Formation of the BCL11A ZF0 Domain
Keywords keywordsSickle cell disease, BCL11A, Tetramerization, hemoglobin, Transcription factor, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.80
Radius of gyration Rg (electron density) rg_electron22.35
Forward intensity I(0) i019609500.00
Molecular weight molecular_weight32760.0 kDa
Excluded volume excluded_volume40721 ų
Envelope volume envelope_volume53566 ų
Hydration-shell volume shell_volume20580 ų
Envelope diameter envelope_diameter76.7
Shell Rg shell_rg28.47
Envelope Rg envelope_rg22.09
Shape Rg shape_rg22.38
Total Rg total_rg23.12
Total atoms total_atoms2234
Residues n_residues279
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 dmax74.6
Rg (real space) rg_real22.73
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.9610e+07
I(0) uncertainty (real space) i0_real_error2.7150e+05
Rg (reciprocal space) rg_reciprocal22.75
I(0) (reciprocal space) i0_reciprocal19610000.0000
Solution quality estimate total_estimate0.8980
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha936400.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)