9rsx

Structure of RACK1 bound to the C-terminus of SERBP1 and the RIH region of ZAK

Method: ELECTRON MICROSCOPY Dmax: 68.5 Å Quality: GOOD

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

Mitogen-activated protein kinase kinase kinase 20

OrganismNot specified

UniProt Q9NYL2

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N2; UniProt 1–800 Not recorded Plasminogen activator inhibitor 1 RNA-binding protein × 1 (Q8NC51) 40S ribosomal protein S3 × 1 (P23396) Receptor of activated protein C kinase 1 × 1 (P63244) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.91 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M3K20_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain N2; PDBConstruct 1–800; UniProt 1–800

Plasminogen activator inhibitor 1 RNA-binding protein

OrganismNot specified

UniProt Q8NC51

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N3; UniProt 1–408 Not recorded Mitogen-activated protein kinase kinase kinase 20 × 1 (Q9NYL2) 40S ribosomal protein S3 × 1 (P23396) Receptor of activated protein C kinase 1 × 1 (P63244) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.91 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAIRB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain N3; PDBConstruct 1–408; UniProt 1–408

40S ribosomal protein S3

OrganismNot specified

UniProt P23396

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain RD; UniProt 1–243 Not recorded Mitogen-activated protein kinase kinase kinase 20 × 1 (Q9NYL2) Plasminogen activator inhibitor 1 RNA-binding protein × 1 (Q8NC51) Receptor of activated protein C kinase 1 × 1 (P63244) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.91 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.

186 other PDB entries and 191 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain RD; PDBConstruct 1–243; UniProt 1–243

Receptor of activated protein C kinase 1

OrganismNot specified

UniProt P63244

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain Rg; UniProt 1–317 Not recorded Mitogen-activated protein kinase kinase kinase 20 × 1 (Q9NYL2) Plasminogen activator inhibitor 1 RNA-binding protein × 1 (Q8NC51) 40S ribosomal protein S3 × 1 (P23396) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.91 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.

187 other PDB entries and 194 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RACK1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain Rg; PDBConstruct 1–317; UniProt 1–317

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 9rsx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rsx
Deposition date deposition_date2025-07-01
Structure title titleStructure of RACK1 bound to the C-terminus of SERBP1 and the RIH region of ZAK
Keywords keywordsZAK, collision, RSR, quality control, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier20.62
Radius of gyration Rg (electron density) rg_electron19.53
Forward intensity I(0) i026508300.00
Molecular weight molecular_weight38844.0 kDa
Excluded volume excluded_volume48342 ų
Envelope volume envelope_volume55764 ų
Hydration-shell volume shell_volume23054 ų
Envelope diameter envelope_diameter69.5
Shell Rg shell_rg26.98
Envelope Rg envelope_rg19.94
Shape Rg shape_rg19.50
Total Rg total_rg20.55
Total atoms total_atoms2733
Residues n_residues353
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 dmax68.5
Rg (real space) rg_real20.49
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.6510e+07
I(0) uncertainty (real space) i0_real_error3.0050e+05
Rg (reciprocal space) rg_reciprocal20.52
I(0) (reciprocal space) i0_reciprocal26510000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.169
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6992000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.795; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)