7jzv

Cryo-EM structure of the BRCA1-UbcH5c/BARD1 E3-E2 module bound to a nucleosome

Method: ELECTRON MICROSCOPY Dmax: 121.3 Å Quality: EXCELLENT

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

BRCA1,Ubiquitin-conjugating enzyme E2 D3

Homo sapiens

UniProt A0A386IN42

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 2–104 Mutation:UbcH5c C85K BRCA1-associated RING domain protein 1 × 1 (Q99728) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-K × 2 (O60814) Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A386IN42_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–105; UniProt 2–104

BRCA1,Ubiquitin-conjugating enzyme E2 D3

Homo sapiens

UniProt P61077

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 2–147 Mutation:UbcH5c C85K BRCA1-associated RING domain protein 1 × 1 (Q99728) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-K × 2 (O60814) Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

45 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 113–258; UniProt 2–147

BRCA1-associated RING domain protein 1

Homo sapiens

UniProt Q99728

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 26–140 Not recorded BRCA1,Ubiquitin-conjugating enzyme E2 D3 × 1 (A0A386IN42,P61077) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-K × 2 (O60814) Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BARD1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–115; UniProt 26–140

Histone H2A type 2-A

Homo sapiens

UniProt Q6FI13

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain N; UniProt 2–130 Chain n; UniProt 2–130 Not recorded BRCA1,Ubiquitin-conjugating enzyme E2 D3 × 1 (A0A386IN42,P61077) BRCA1-associated RING domain protein 1 × 1 (Q99728) Histone H2B type 1-K × 2 (O60814) Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

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

View Construct and Data Evidence
UniProt name H2A2A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 5–133; UniProt 2–130 Author chain n; PDBConstruct 5–133; UniProt 2–130

Histone H2B type 1-K

Homo sapiens

UniProt O60814

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain O; UniProt 2–126 Chain o; UniProt 2–126 Not recorded BRCA1,Ubiquitin-conjugating enzyme E2 D3 × 1 (A0A386IN42,P61077) BRCA1-associated RING domain protein 1 × 1 (Q99728) Histone H2A type 2-A × 2 (Q6FI13) Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain O; PDBConstruct 1–125; UniProt 2–126 Author chain o; PDBConstruct 1–125; UniProt 2–126

Histone H3.2

Homo sapiens

UniProt Q71DI3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain P; UniProt 2–136 Chain p; UniProt 2–136 Mutation:C110A BRCA1,Ubiquitin-conjugating enzyme E2 D3 × 1 (A0A386IN42,P61077) BRCA1-associated RING domain protein 1 × 1 (Q99728) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-K × 2 (O60814) Histone H4 × 2 (P62805) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–135; UniProt 2–136 Author chain p; PDBConstruct 1–135; UniProt 2–136

Histone H4

Homo sapiens

UniProt P62805

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain Q; UniProt 2–103 Chain q; UniProt 2–103 Not recorded BRCA1,Ubiquitin-conjugating enzyme E2 D3 × 1 (A0A386IN42,P61077) BRCA1-associated RING domain protein 1 × 1 (Q99728) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-K × 2 (O60814) Histone H3.2 × 2 (Q71DI3) Widom 601 153-bp × 1 Widom 601 153-bp × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain Q; PDBConstruct 1–102; UniProt 2–103 Author chain q; PDBConstruct 1–102; UniProt 2–103

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 7jzv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7jzv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7jzv
Deposition date deposition_date2020-09-02
Structure title titleCryo-EM structure of the BRCA1-UbcH5c/BARD1 E3-E2 module bound to a nucleosome
Keywords keywordsComplex, Ubiquitin, Nucleosome, RING, ligase, LIGASE-DNA complex; LIGASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.41
Radius of gyration Rg (electron density) rg_electron39.31
Forward intensity I(0) i01065070000.00
Molecular weight molecular_weight209440.0 kDa
Excluded volume excluded_volume237820 ų
Envelope volume envelope_volume359820 ų
Hydration-shell volume shell_volume73564 ų
Envelope diameter envelope_diameter124.0
Shell Rg shell_rg47.30
Envelope Rg envelope_rg38.56
Shape Rg shape_rg39.20
Total Rg total_rg39.90
Total atoms total_atoms14339
Residues n_residues1371
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 dmax121.3
Rg (real space) rg_real41.14
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.0650e+09
I(0) uncertainty (real space) i0_real_error1.6860e+07
Rg (reciprocal space) rg_reciprocal41.41
I(0) (reciprocal space) i0_reciprocal1065000000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.2
Skewness Skewness skewness0.006
Kurtosis Kurtosis kurtosis-0.630
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71420000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7jzvA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id7jzvA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme

8. Citations (1)

9. Files and Curves (10)