6ven

Yeast COMPASS in complex with a ubiquitinated nucleosome

Method: ELECTRON MICROSCOPY Dmax: 163.0 Å Quality: GOOD

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Mutation:K4(NLE), M90(NLE), M120(NLE), G102A Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

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–DNA Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Mutation:G99R, A123S Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Mutation:K120C, S30T Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

Ubiquitin

Homo sapiens

UniProt P0CG48

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain K; UniProt 1–76 Mutation:G76C Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 5–80; UniProt 1–76

COMPASS component SWD3

Saccharomyces cerevisiae

UniProt P38123

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain L; UniProt 1–315 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SWD3_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–315; UniProt 1–315

COMPASS component SWD1

Saccharomyces cerevisiae

UniProt P39706

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain M; UniProt 1–426 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SWD1_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–426; UniProt 1–426

Histone-lysine N-methyltransferase, H3 lysine-4 specific

Saccharomyces cerevisiae

UniProt P38827

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain N; UniProt 762–1080 Fragment:UNP residues 762-1080 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SET1_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain N; PDBConstruct 40–358; UniProt 762–1080

COMPASS component BRE2

Saccharomyces cerevisiae

UniProt P43132

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain O; UniProt 1–505 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component SDC1 × 2 (Q03323) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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.

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

View Construct and Data Evidence
UniProt name BRE2_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain O; PDBConstruct 1–505; UniProt 1–505

COMPASS component SDC1

Saccharomyces cerevisiae

UniProt Q03323

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain P; UniProt 1–175 Chain Q; UniProt 1–175 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SPP1 × 1 (Q03012) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDC1_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain P; PDBConstruct 1–175; UniProt 1–175 Author chain Q; PDBConstruct 1–175; UniProt 1–175

COMPASS component SPP1

Saccharomyces cerevisiae

UniProt Q03012

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 Heteromer Protein × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain R; UniProt 2–353 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) 601 DNA (146-MER) × 1 601 DNA (146-MER) × 1 Ubiquitin × 1 (P0CG48) COMPASS component SWD3 × 1 (P38123) COMPASS component SWD1 × 1 (P39706) Histone-lysine N-methyltransferase, H3 lysine-4 specific × 1 (P38827) COMPASS component BRE2 × 1 (P43132) COMPASS component SDC1 × 2 (Q03323) ZN ZINC ION × 1 SAM S-ADENOSYLMETHIONINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot force 5 3.5 sec blot time Resolution 3.37 Å

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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPP1_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain R; PDBConstruct 40–391; UniProt 2–353

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 6ven

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ven
Deposition date deposition_date2020-01-02
Structure title titleYeast COMPASS in complex with a ubiquitinated nucleosome
Keywords keywordsMethylation, histone, transcription, ubiquitin, gene regulation, TRANSFERASE-STRUCTURAL PROTEIN-DNA complex; TRANSFERASE/STRUCTURAL PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.99
Radius of gyration Rg (electron density) rg_electron50.32
Forward intensity I(0) i02384230000.00
Molecular weight molecular_weight346790.0 kDa
Excluded volume excluded_volume408720 ų
Envelope volume envelope_volume641880 ų
Hydration-shell volume shell_volume103590 ų
Envelope diameter envelope_diameter176.1
Shell Rg shell_rg56.58
Envelope Rg envelope_rg49.24
Shape Rg shape_rg50.30
Total Rg total_rg50.57
Total atoms total_atoms24028
Residues n_residues2558
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 dmax163.0
Rg (real space) rg_real50.83
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real2.3840e+09
I(0) uncertainty (real space) i0_real_error4.2360e+07
Rg (reciprocal space) rg_reciprocal51.12
I(0) (reciprocal space) i0_reciprocal2385000000.0000
Solution quality estimate total_estimate0.8738
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.3
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha418600000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.745

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6venB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6venC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6venD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6venF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6venG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6venH00
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)