6yn1

Crystal structure of histone chaperone APLF acidic domain bound to the histone H2A-H2B-H3-H4 octamer

Method: X-RAY DIFFRACTION Dmax: 150.1 Å Quality: GOOD

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

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

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 14–119 Chain F; UniProt 14–119 Not recorded Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain K; UniProt 14–119 Chain P; UniProt 14–119 Not recorded Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain U; UniProt 14–119 Chain Z; UniProt 14–119 Not recorded Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
4 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain e; UniProt 14–119 Chain j; UniProt 14–119 Not recorded Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233

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.

226 other PDB entries and 235 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–107; UniProt 14–119 Author chain F; PDBConstruct 2–107; UniProt 14–119 Author chain K; PDBConstruct 2–107; UniProt 14–119 Author chain P; PDBConstruct 2–107; UniProt 14–119 Author chain U; PDBConstruct 2–107; UniProt 14–119 Author chain Z; PDBConstruct 2–107; UniProt 14–119 Author chain e; PDBConstruct 2–107; UniProt 14–119 Author chain j; PDBConstruct 2–107; UniProt 14–119

Histone H2B

Xenopus laevis

UniProt A0A1L8FQA5

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 28–126 Chain G; UniProt 28–126 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain L; UniProt 28–126 Chain Q; UniProt 28–126 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain V; UniProt 28–126 Chain a; UniProt 28–126 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
4 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain f; UniProt 28–126 Chain k; UniProt 28–126 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1L8FQA5_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–100; UniProt 28–126 Author chain G; PDBConstruct 2–100; UniProt 28–126 Author chain L; PDBConstruct 2–100; UniProt 28–126 Author chain Q; PDBConstruct 2–100; UniProt 28–126 Author chain V; PDBConstruct 2–100; UniProt 28–126 Author chain a; PDBConstruct 2–100; UniProt 28–126 Author chain f; PDBConstruct 2–100; UniProt 28–126 Author chain k; PDBConstruct 2–100; UniProt 28–126

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

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 39–136 Chain H; UniProt 39–136 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain M; UniProt 39–136 Chain R; UniProt 39–136 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain W; UniProt 39–136 Chain b; UniProt 39–136 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
4 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain g; UniProt 39–136 Chain l; UniProt 39–136 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H4 × 2 (P62799) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233

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.

126 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–99; UniProt 39–136 Author chain H; PDBConstruct 2–99; UniProt 39–136 Author chain M; PDBConstruct 2–99; UniProt 39–136 Author chain R; PDBConstruct 2–99; UniProt 39–136 Author chain W; PDBConstruct 2–99; UniProt 39–136 Author chain b; PDBConstruct 2–99; UniProt 39–136 Author chain g; PDBConstruct 2–99; UniProt 39–136 Author chain l; PDBConstruct 2–99; UniProt 39–136

Histone H4

Xenopus laevis

UniProt P62799

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 D; UniProt 21–103 Chain I; UniProt 21–103 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain N; UniProt 21–103 Chain S; UniProt 21–103 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain X; UniProt 21–103 Chain c; UniProt 21–103 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
4 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain h; UniProt 21–103 Chain m; UniProt 21–103 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Aprataxin and PNK-like factor × 2 (Q8IW19) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233

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.

354 other PDB entries and 367 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–84; UniProt 21–103 Author chain I; PDBConstruct 2–84; UniProt 21–103 Author chain N; PDBConstruct 2–84; UniProt 21–103 Author chain S; PDBConstruct 2–84; UniProt 21–103 Author chain X; PDBConstruct 2–84; UniProt 21–103 Author chain c; PDBConstruct 2–84; UniProt 21–103 Author chain h; PDBConstruct 2–84; UniProt 21–103 Author chain m; PDBConstruct 2–84; UniProt 21–103

Aprataxin and PNK-like factor

Homo sapiens

UniProt Q8IW19

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 E; UniProt 449–490 Chain J; UniProt 449–490 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain O; UniProt 449–490 Chain T; UniProt 449–490 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain Y; UniProt 449–490 Chain d; UniProt 449–490 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233
4 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain i; UniProt 449–490 Chain n; UniProt 449–490 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M sodium cacodylate pH6.5, 1.0 M tri-sodium citrate Resolution 2.35 Å R-free 0.233

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.

10 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APLF_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 2–43; UniProt 449–490 Author chain J; PDBConstruct 2–43; UniProt 449–490 Author chain O; PDBConstruct 2–43; UniProt 449–490 Author chain T; PDBConstruct 2–43; UniProt 449–490 Author chain Y; PDBConstruct 2–43; UniProt 449–490 Author chain d; PDBConstruct 2–43; UniProt 449–490 Author chain i; PDBConstruct 2–43; UniProt 449–490 Author chain n; PDBConstruct 2–43; UniProt 449–490

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 6yn1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6yn1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6yn1
Deposition date deposition_date2020-04-10
Structure title titleCrystal structure of histone chaperone APLF acidic domain bound to the histone H2A-H2B-H3-H4 octamer
Keywords keywordsOctamer, aplf, chaperone, histone; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.03
Radius of gyration Rg (electron density) rg_electron47.15
Forward intensity I(0) i01718140000.00
Molecular weight molecular_weight348400.0 kDa
Excluded volume excluded_volume438850 ų
Envelope volume envelope_volume595080 ų
Hydration-shell volume shell_volume100900 ų
Envelope diameter envelope_diameter155.0
Shell Rg shell_rg54.93
Envelope Rg envelope_rg46.05
Shape Rg shape_rg47.17
Total Rg total_rg47.36
Total atoms total_atoms24541
Residues n_residues3071
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 dmax150.1
Rg (real space) rg_real47.66
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.7180e+09
I(0) uncertainty (real space) i0_real_error3.2140e+07
Rg (reciprocal space) rg_reciprocal48.02
I(0) (reciprocal space) i0_reciprocal1719000000.0000
Solution quality estimate total_estimate0.8915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.7
Skewness Skewness skewness0.060
Kurtosis Kurtosis kurtosis-0.584
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha555000000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.911

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 18 domains

CATH v4.4 (18 domains)

Domain ID domain_id6yn1B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1G01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1H01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1L01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1M01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1Q01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1R01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1V01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1W01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1X01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1a01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1b01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1c01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1f01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1g01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1k01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6yn1l01
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)