6see

Class2A : CENP-A nucleosome in complex with CENP-C central region

Method: ELECTRON MICROSCOPY Dmax: 124.0 Å Quality: REASONABLE

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

Histone H3-like centromeric protein A

Homo sapiens

UniProt P49450

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–140 Chain E; UniProt 1–140 Not recorded Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Centromere protein C × 1 (Q03188) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

33 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–140; UniProt 1–140 Author chain E; PDBConstruct 1–140; UniProt 1–140

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 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Centromere protein C × 1 (Q03188) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

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 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Centromere protein C × 1 (Q03188) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 C; PDBConstruct 1–130; UniProt 1–130 Author chain G; PDBConstruct 1–130; UniProt 1–130

Histone H2B type 1-C/E/F/G/I

Homo sapiens

UniProt P62807

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) DNA (145-MER) × 1 DNA (145-MER) × 1 Centromere protein C × 1 (Q03188) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126

Centromere protein C

Homo sapiens

UniProt Q03188

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain V; UniProt 426–537 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPC_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain V; PDBConstruct 13–124; UniProt 426–537

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 6see

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6see
Deposition date deposition_date2019-07-29
Structure title titleClass2A : CENP-A nucleosome in complex with CENP-C central region
Keywords keywordsCENP-A, nucleosome, centromere, centromeric chromatin, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.61
Radius of gyration Rg (electron density) rg_electron37.79
Forward intensity I(0) i0820295000.00
Molecular weight molecular_weight174990.0 kDa
Excluded volume excluded_volume194240 ų
Envelope volume envelope_volume292840 ų
Hydration-shell volume shell_volume63717 ų
Envelope diameter envelope_diameter125.5
Shell Rg shell_rg44.79
Envelope Rg envelope_rg37.05
Shape Rg shape_rg37.61
Total Rg total_rg38.52
Total atoms total_atoms11949
Residues n_residues1046
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 dmax124.0
Rg (real space) rg_real40.44
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real8.2030e+08
I(0) uncertainty (real space) i0_real_error1.3660e+07
Rg (reciprocal space) rg_reciprocal40.61
I(0) (reciprocal space) i0_reciprocal820400000.0000
Solution quality estimate total_estimate0.6774
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.639
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55120000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.984; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)