9g8r

human SKI7-SKI238 complex in the open state

Method: ELECTRON MICROSCOPY Dmax: 164.9 Å Quality: GOOD

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

Superkiller complex protein 3

Homo sapiens

UniProt Q6PGP7

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–1564 Not recorded WD repeat-containing protein 61 × 2 (Q9GZS3) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Superkiller complex protein 2 × 1 (Q15477) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKI3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 5–1568; UniProt 1–1564

WD repeat-containing protein 61

Homo sapiens

UniProt Q9GZS3

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–305 Chain D; UniProt 1–305 Not recorded Superkiller complex protein 3 × 1 (Q6PGP7) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Superkiller complex protein 2 × 1 (Q15477) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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.

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

View Construct and Data Evidence
UniProt name WDR61_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–305; UniProt 1–305 Author chain D; PDBConstruct 1–305; UniProt 1–305

Isoform 2 of HBS1-like protein

Homo sapiens

UniProt Q9Y450

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 372–546 Not recorded Superkiller complex protein 3 × 1 (Q6PGP7) WD repeat-containing protein 61 × 2 (Q9GZS3) Superkiller complex protein 2 × 1 (Q15477) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HBS1L_HUMAN
Isoform Q9Y450-2
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 5–179; UniProt 372–546

Superkiller complex protein 2

Homo sapiens

UniProt Q15477

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–774 Chain A; UniProt 1049–1246 Not recorded Superkiller complex protein 3 × 1 (Q6PGP7) WD repeat-containing protein 61 × 2 (Q9GZS3) Isoform 2 of HBS1-like protein × 1 (Q9Y450) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKI2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–774; UniProt 1–774 Author chain A; PDBConstruct 779–976; UniProt 1049–1246

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 9g8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9g8r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9g8r
Deposition date deposition_date2024-07-23
Structure title titlehuman SKI7-SKI238 complex in the open state
Keywords keywordsHelicase, RNA-binding, RNA-degradation, cytoplasm, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.10
Radius of gyration Rg (electron density) rg_electron48.51
Forward intensity I(0) i0641407000.00
Molecular weight molecular_weight210690.0 kDa
Excluded volume excluded_volume264430 ų
Envelope volume envelope_volume382700 ų
Hydration-shell volume shell_volume69613 ų
Envelope diameter envelope_diameter178.2
Shell Rg shell_rg48.85
Envelope Rg envelope_rg48.61
Shape Rg shape_rg48.48
Total Rg total_rg48.61
Total atoms total_atoms14837
Residues n_residues1900
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 dmax164.9
Rg (real space) rg_real48.58
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real6.4140e+08
I(0) uncertainty (real space) i0_real_error1.3010e+07
Rg (reciprocal space) rg_reciprocal48.11
I(0) (reciprocal space) i0_reciprocal641000000.0000
Solution quality estimate total_estimate0.8237
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.0
Skewness Skewness skewness0.602
Kurtosis Kurtosis kurtosis-0.012
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44570000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.767; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.424

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)