8d0k

Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback template - PRIM2C advanced PIC

Method: ELECTRON MICROSCOPY Dmax: 229.5 Å Quality: GOOD

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

CST complex subunit CTC1

Homo sapiens

UniProt Q2NKJ3

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 2–1217 Not recorded CST complex subunit STN1 × 1 (Q9H668) CST complex subunit TEN1 × 1 (Q86WV5) DNA primase small subunit × 1 (P49642) DNA primase large subunit × 1 (P49643) DNA polymerase alpha catalytic subunit × 1 (P09884) DNA polymerase alpha subunit B × 1 (Q14181) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 31–1246; UniProt 2–1217

CST complex subunit STN1

Homo sapiens

UniProt Q9H668

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain B; UniProt 2–368 Not recorded CST complex subunit CTC1 × 1 (Q2NKJ3) CST complex subunit TEN1 × 1 (Q86WV5) DNA primase small subunit × 1 (P49642) DNA primase large subunit × 1 (P49643) DNA polymerase alpha catalytic subunit × 1 (P09884) DNA polymerase alpha subunit B × 1 (Q14181) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 8–374; UniProt 2–368

CST complex subunit TEN1

Homo sapiens

UniProt Q86WV5

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain C; UniProt 3–123 Not recorded CST complex subunit CTC1 × 1 (Q2NKJ3) CST complex subunit STN1 × 1 (Q9H668) DNA primase small subunit × 1 (P49642) DNA primase large subunit × 1 (P49643) DNA polymerase alpha catalytic subunit × 1 (P09884) DNA polymerase alpha subunit B × 1 (Q14181) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TEN1L_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 32–152; UniProt 3–123

DNA primase small subunit

Homo sapiens

UniProt P49642

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain D; UniProt 2–420 Not recorded CST complex subunit CTC1 × 1 (Q2NKJ3) CST complex subunit STN1 × 1 (Q9H668) CST complex subunit TEN1 × 1 (Q86WV5) DNA primase large subunit × 1 (P49643) DNA polymerase alpha catalytic subunit × 1 (P09884) DNA polymerase alpha subunit B × 1 (Q14181) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

22 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRI1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 16–434; UniProt 2–420

DNA primase large subunit

Homo sapiens

UniProt P49643

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain E; UniProt 2–509 Not recorded CST complex subunit CTC1 × 1 (Q2NKJ3) CST complex subunit STN1 × 1 (Q9H668) CST complex subunit TEN1 × 1 (Q86WV5) DNA primase small subunit × 1 (P49642) DNA polymerase alpha catalytic subunit × 1 (P09884) DNA polymerase alpha subunit B × 1 (Q14181) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

21 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRI2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 16–523; UniProt 2–509

DNA polymerase alpha catalytic subunit

Homo sapiens

UniProt P09884

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain F; UniProt 2–1462 Not recorded CST complex subunit CTC1 × 1 (Q2NKJ3) CST complex subunit STN1 × 1 (Q9H668) CST complex subunit TEN1 × 1 (Q86WV5) DNA primase small subunit × 1 (P49642) DNA primase large subunit × 1 (P49643) DNA polymerase alpha subunit B × 1 (Q14181) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

21 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOLA_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 66–1526; UniProt 2–1462

DNA polymerase alpha subunit B

Homo sapiens

UniProt Q14181

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 × 7 DNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain G; UniProt 2–598 Not recorded CST complex subunit CTC1 × 1 (Q2NKJ3) CST complex subunit STN1 × 1 (Q9H668) CST complex subunit TEN1 × 1 (Q86WV5) DNA primase small subunit × 1 (P49642) DNA primase large subunit × 1 (P49643) DNA polymerase alpha catalytic subunit × 1 (P09884) ;DNA (5'-D(P*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*A)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is only added just before sample vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.27 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.

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

View Construct and Data Evidence
UniProt name DPOA2_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 16–612; UniProt 2–598

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 8d0k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d0k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8d0k
Deposition date deposition_date2022-05-26
Structure title titleHuman CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback template - PRIM2C advanced PIC
Keywords keywordstelomere, C-strand, complex, 4xTEL-foldback DNA template, PRIM2C, REPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.73
Radius of gyration Rg (electron density) rg_electron64.14
Forward intensity I(0) i02698730000.00
Molecular weight molecular_weight440950.0 kDa
Excluded volume excluded_volume553670 ų
Envelope volume envelope_volume918220 ų
Hydration-shell volume shell_volume122320 ų
Envelope diameter envelope_diameter233.7
Shell Rg shell_rg63.10
Envelope Rg envelope_rg62.07
Shape Rg shape_rg64.16
Total Rg total_rg64.04
Total atoms total_atoms31011
Residues n_residues3840
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 dmax229.5
Rg (real space) rg_real63.86
Rg uncertainty (real space) rg_real_error3.40
I(0) (real space) i0_real2.6990e+09
I(0) uncertainty (real space) i0_real_error6.0780e+07
Rg (reciprocal space) rg_reciprocal63.59
I(0) (reciprocal space) i0_reciprocal2697000000.0000
Solution quality estimate total_estimate0.8570
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.4
Skewness Skewness skewness0.383
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha234900000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)