6voy

Cryo-EM structure of HTLV-1 instasome

Method: ELECTRON MICROSCOPY Dmax: 165.3 Å Quality: GOOD

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

DNA-binding protein 7d

Human T-cell leukemia virus type I

UniProt A0A1Y1CAW1

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 × 6 DNA 6 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 569–863 Chain B; UniProt 569–863 Chain C; UniProt 569–863 Chain D; UniProt 569–863 Mutation:W24A Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 2 (Q13362) ;DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3') ; × 2 DNA (25-MER) × 2 ;DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3') ; × 2 ZN ZINC ION × 4 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.70 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 A0A1Y1CAW1_9DELA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 96–390; UniProt 569–863 Author chain B; PDBConstruct 96–390; UniProt 569–863 Author chain C; PDBConstruct 96–390; UniProt 569–863 Author chain D; PDBConstruct 96–390; UniProt 569–863

DNA-binding protein 7d

Human T-cell leukemia virus type I

UniProt P39476

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 × 6 DNA 6 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–64 Chain B; UniProt 1–64 Chain C; UniProt 1–64 Chain D; UniProt 1–64 Mutation:W24A Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 2 (Q13362) ;DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3') ; × 2 DNA (25-MER) × 2 ;DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3') ; × 2 ZN ZINC ION × 4 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.70 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 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DN7D_SACS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–84; UniProt 1–64 Author chain B; PDBConstruct 21–84; UniProt 1–64 Author chain C; PDBConstruct 21–84; UniProt 1–64 Author chain D; PDBConstruct 21–84; UniProt 1–64

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Homo sapiens

UniProt Q13362

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 × 6 DNA 6 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 30–372 Chain F; UniProt 30–372 Not recorded DNA-binding protein 7d × 4 (P39476,A0A1Y1CAW1) ;DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3') ; × 2 DNA (25-MER) × 2 ;DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3') ; × 2 ZN ZINC ION × 4 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.70 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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2A5G_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–343; UniProt 30–372 Author chain F; PDBConstruct 1–343; UniProt 30–372

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 6voy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6voy
Deposition date deposition_date2020-02-01
Structure title titleCryo-EM structure of HTLV-1 instasome
Keywords keywordsIntegrase, Intasome, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.76
Radius of gyration Rg (electron density) rg_electron49.35
Forward intensity I(0) i01172770000.00
Molecular weight molecular_weight252150.0 kDa
Excluded volume excluded_volume301940 ų
Envelope volume envelope_volume480700 ų
Hydration-shell volume shell_volume82412 ų
Envelope diameter envelope_diameter165.1
Shell Rg shell_rg51.44
Envelope Rg envelope_rg49.00
Shape Rg shape_rg49.34
Total Rg total_rg49.46
Total atoms total_atoms17556
Residues n_residues1904
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 dmax165.3
Rg (real space) rg_real48.78
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real1.1730e+09
I(0) uncertainty (real space) i0_real_error1.9300e+07
Rg (reciprocal space) rg_reciprocal48.76
I(0) (reciprocal space) i0_reciprocal1173000000.0000
Solution quality estimate total_estimate0.8764
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.6
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha99210000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6voyE00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id6voyF00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)