9ubd

The Structural Basis of the Recognition of the Histone Variant H2A.Z by the SRCAP Catalytic Subunit

Method: X-RAY DIFFRACTION Dmax: 80.3 Å Quality: GOOD

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

Histone H2A.Z

Homo sapiens

UniProt P0C0S5

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 17–114 Chain D; UniProt 17–114 Not recorded Histone H2B type 1-J × 4 (P06899) Helicase SRCAP × 2 (Q6ZRS2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2 M Potassium thiocyanate 15 % w/v PEG 3,350 pH 7.0 Resolution 2.53 Å R-free 0.288

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 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AZ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–98; UniProt 17–114 Author chain D; PDBConstruct 1–98; UniProt 17–114

Histone H2B type 1-J

Homo sapiens

UniProt P06899

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 34–125 Chain E; UniProt 34–125 Not recorded Histone H2A.Z × 4 (P0C0S5) Helicase SRCAP × 2 (Q6ZRS2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2 M Potassium thiocyanate 15 % w/v PEG 3,350 pH 7.0 Resolution 2.53 Å R-free 0.288

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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–92; UniProt 34–125 Author chain E; PDBConstruct 1–92; UniProt 34–125

Helicase SRCAP

OrganismNot specified

UniProt Q6ZRS2

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 531–560 Not recorded Histone H2A.Z × 4 (P0C0S5) Histone H2B type 1-J × 4 (P06899) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2 M Potassium thiocyanate 15 % w/v PEG 3,350 pH 7.0 Resolution 2.53 Å R-free 0.288

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRCAP_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–30; UniProt 531–560

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 9ubd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ubd
Deposition date deposition_date2025-04-02
最后修订 last_revision2026-04-08
Structure title titleThe Structural Basis of the Recognition of the Histone Variant H2A.Z by the SRCAP Catalytic Subunit
Keywords keywordsHistone, Histone Variant, histone fold domain, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.30
Radius of gyration Rg (electron density) rg_electron23.30
Forward intensity I(0) i024692200.00
Molecular weight molecular_weight37551.0 kDa
Excluded volume excluded_volume46909 ų
Envelope volume envelope_volume58034 ų
Hydration-shell volume shell_volume21369 ų
Envelope diameter envelope_diameter81.0
Shell Rg shell_rg29.28
Envelope Rg envelope_rg23.35
Shape Rg shape_rg23.30
Total Rg total_rg24.06
Total atoms total_atoms2650
Residues n_residues365
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 dmax80.3
Rg (real space) rg_real24.30
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real2.4690e+07
I(0) uncertainty (real space) i0_real_error3.7340e+05
Rg (reciprocal space) rg_reciprocal24.30
I(0) (reciprocal space) i0_reciprocal24690000.0000
Solution quality estimate total_estimate0.8934
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.5
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3996000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)