4cay

Crystal structure of a human Anp32e-H2A.Z-H2B complex

Method: X-RAY DIFFRACTION Dmax: 67.2 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 19–128 Fragment:GLOBULAR DOMAIN, RESIDUES 19-128 HISTONE H2B TYPE 1-J × 1 (P06899) ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER E × 1 (Q9BTT0) X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M NA CACODYLATE, PH 7.0, 0.2 M NA FORMATE, 24% TO 30% PEG 3350 Resolution 1.48 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.

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 2–111; UniProt 19–128

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 31–126 Fragment:GLOBULAR DOMAIN, RESIDUES 31-126 HISTONE H2A.Z × 1 (P0C0S5) ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER E × 1 (Q9BTT0) X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M NA CACODYLATE, PH 7.0, 0.2 M NA FORMATE, 24% TO 30% PEG 3350 Resolution 1.48 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.

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 2–97; UniProt 31–126

ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER E

HOMO SAPIENS

UniProt Q9BTT0

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 C; UniProt 215–240 Fragment:H2A.Z INTERACTING DOMAIN (ZID), RESIDUES 215-240 HISTONE H2A.Z × 1 (P0C0S5) HISTONE H2B TYPE 1-J × 1 (P06899) X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M NA CACODYLATE, PH 7.0, 0.2 M NA FORMATE, 24% TO 30% PEG 3350 Resolution 1.48 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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AN32E_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 5–30; UniProt 215–240

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 4cay

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4cay
Deposition date deposition_date2013-10-09
Structure title titleCrystal structure of a human Anp32e-H2A.Z-H2B complex
Keywords keywordsEPIGENETICS, TRANSCRIPTION, NUCLEOSOME, HISTONE VARIANT, HISTONE CHAPERONE; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.47
Radius of gyration Rg (electron density) rg_electron17.13
Forward intensity I(0) i09153040.00
Molecular weight molecular_weight22206.0 kDa
Excluded volume excluded_volume27834 ų
Envelope volume envelope_volume32067 ų
Hydration-shell volume shell_volume15974 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg23.09
Envelope Rg envelope_rg17.66
Shape Rg shape_rg17.11
Total Rg total_rg18.17
Total atoms total_atoms1563
Residues n_residues201
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 dmax67.2
Rg (real space) rg_real18.45
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real9.1530e+06
I(0) uncertainty (real space) i0_real_error1.2930e+05
Rg (reciprocal space) rg_reciprocal18.45
I(0) (reciprocal space) i0_reciprocal9153000.0000
Solution quality estimate total_estimate0.8303
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.110
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2060000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.629; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4caya_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd4cayb_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones

CATH v4.4 (2 domains)

Domain ID domain_id4cayA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4cayB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)