7oug

STLV-1 intasome:B56 in complex with the strand-transfer inhibitor raltegravir

Method: ELECTRON MICROSCOPY Dmax: 152.6 Å Quality: GOOD

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

Integrase

Simian T-lymphotropic virus 1

UniProt Q4QY51

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 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 597–896 Chain B; UniProt 597–896 Chain D; UniProt 597–896 Chain E; UniProt 597–896 Mutation:A219E ;Isoform 3 of PC4 and SFRS1-interacting protein,Isoform Gamma-2 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform ; × 2 (O75475,Q13362) ;DNA (5'-D(*AP*CP*TP*GP*TP*GP*TP*TP*TP*GP*GP*CP*GP*CP*TP*TP*CP*TP*CP*TP*C)-3') ; × 2 ;DNA (5'-D(*GP*AP*GP*AP*GP*AP*AP*GP*CP*GP*CP*CP*AP*AP*AP*CP*AP*CP*A)-3') ; × 2 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 RLT N-(4-fluorobenzyl)-5-hydroxy-1-methyl-2-(1-methyl-1-{[(5-methyl-1,3,4-oxadiazol-2-yl)carbonyl]amino}ethyl)-6-oxo-1,6-di hydropyrimidine-4-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q4QY51_9STL1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–301; UniProt 597–896 Author chain B; PDBConstruct 2–301; UniProt 597–896 Author chain D; PDBConstruct 2–301; UniProt 597–896 Author chain E; PDBConstruct 2–301; UniProt 597–896

;Isoform 3 of PC4 and SFRS1-interacting protein,Isoform Gamma-2 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform ;

Homo sapiens

UniProt O75475

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 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 1–325 Chain F; UniProt 1–325 Not recorded Integrase × 4 (Q4QY51) ;DNA (5'-D(*AP*CP*TP*GP*TP*GP*TP*TP*TP*GP*GP*CP*GP*CP*TP*TP*CP*TP*CP*TP*C)-3') ; × 2 ;DNA (5'-D(*GP*AP*GP*AP*GP*AP*AP*GP*CP*GP*CP*CP*AP*AP*AP*CP*AP*CP*A)-3') ; × 2 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 RLT N-(4-fluorobenzyl)-5-hydroxy-1-methyl-2-(1-methyl-1-{[(5-methyl-1,3,4-oxadiazol-2-yl)carbonyl]amino}ethyl)-6-oxo-1,6-di hydropyrimidine-4-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

34 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSIP1_HUMAN
Isoform O75475-3
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–326; UniProt 1–325 Author chain F; PDBConstruct 2–326; UniProt 1–325

;Isoform 3 of PC4 and SFRS1-interacting protein,Isoform Gamma-2 of 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 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 11–380 Chain F; UniProt 11–380 Not recorded Integrase × 4 (Q4QY51) ;DNA (5'-D(*AP*CP*TP*GP*TP*GP*TP*TP*TP*GP*GP*CP*GP*CP*TP*TP*CP*TP*CP*TP*C)-3') ; × 2 ;DNA (5'-D(*GP*AP*GP*AP*GP*AP*AP*GP*CP*GP*CP*CP*AP*AP*AP*CP*AP*CP*A)-3') ; × 2 ZN ZINC ION × 4 MG MAGNESIUM ION × 4 RLT N-(4-fluorobenzyl)-5-hydroxy-1-methyl-2-(1-methyl-1-{[(5-methyl-1,3,4-oxadiazol-2-yl)carbonyl]amino}ethyl)-6-oxo-1,6-di hydropyrimidine-4-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 Q13362-3
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 328–697; UniProt 11–380 Author chain F; PDBConstruct 328–697; UniProt 11–380

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 7oug

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7oug
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7oug
Deposition date deposition_date2021-06-11
Structure title titleSTLV-1 intasome:B56 in complex with the strand-transfer inhibitor raltegravir
Keywords keywordsSTLV-intasome, HTLV, integrase strand-transfer inhibitor, raltegravir., VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.27
Radius of gyration Rg (electron density) rg_electron45.68
Forward intensity I(0) i0759842000.00
Molecular weight molecular_weight215010.0 kDa
Excluded volume excluded_volume263660 ų
Envelope volume envelope_volume387530 ų
Hydration-shell volume shell_volume71186 ų
Envelope diameter envelope_diameter160.6
Shell Rg shell_rg49.41
Envelope Rg envelope_rg45.42
Shape Rg shape_rg45.72
Total Rg total_rg45.71
Total atoms total_atoms15082
Residues n_residues1744
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 dmax152.6
Rg (real space) rg_real44.49
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real7.5980e+08
I(0) uncertainty (real space) i0_real_error1.3520e+07
Rg (reciprocal space) rg_reciprocal44.27
I(0) (reciprocal space) i0_reciprocal759600000.0000
Solution quality estimate total_estimate0.8440
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.6
Skewness Skewness skewness0.524
Kurtosis Kurtosis kurtosis-0.220
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94520000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.734; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7ougA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H
Domain ID domain_id7ougB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H
Domain ID domain_id7ougD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H
Domain ID domain_id7ougE01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H

8. Citations (1)

9. Files and Curves (10)