5aff

Symportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA binding site

Method: X-RAY DIFFRACTION Dmax: 103.2 Å Quality: GOOD

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

SYMPORTIN 1

CHAETOMIUM THERMOPHILUM

UniProt G0S5S6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 24–676 Not recorded RIBOSOMAL PROTEIN L5 × 1 (G0SEG2) RIBOSOMAL PROTEIN L11 × 1 (G0SHQ2) X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M SODIUM ACETATE, 8% (V/V) PEG 4000 Resolution 3.40 Å R-free 0.300

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 G0S5S6_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–654; UniProt 24–676

RIBOSOMAL PROTEIN L5

CHAETOMIUM THERMOPHILUM

UniProt G0SEG2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–41 Fragment:N-TERMINUS LINEAR MOTIF, UNP RESIDUES 1-41 SYMPORTIN 1 × 1 (G0S5S6) RIBOSOMAL PROTEIN L11 × 1 (G0SHQ2) X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M SODIUM ACETATE, 8% (V/V) PEG 4000 Resolution 3.40 Å R-free 0.300

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 G0SEG2_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 8–48; UniProt 1–41

RIBOSOMAL PROTEIN L11

CHAETOMIUM THERMOPHILUM

UniProt G0SHQ2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–173 Not recorded SYMPORTIN 1 × 1 (G0S5S6) RIBOSOMAL PROTEIN L5 × 1 (G0SEG2) X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M SODIUM ACETATE, 8% (V/V) PEG 4000 Resolution 3.40 Å R-free 0.300

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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SHQ2_CHATD
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–173; UniProt 1–173

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 5aff

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5aff
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5aff
Deposition date deposition_date2015-01-21
Structure title titleSymportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA binding site
Keywords keywordsCHAPERONE, RIBOSOME BIOGENESIS, ALPHA SOLENOID.; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.75
Radius of gyration Rg (electron density) rg_electron31.30
Forward intensity I(0) i097221700.00
Molecular weight molecular_weight79570.0 kDa
Excluded volume excluded_volume100390 ų
Envelope volume envelope_volume131160 ų
Hydration-shell volume shell_volume36092 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg37.10
Envelope Rg envelope_rg31.44
Shape Rg shape_rg31.28
Total Rg total_rg31.91
Total atoms total_atoms5606
Residues n_residues712
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 dmax103.2
Rg (real space) rg_real31.82
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real9.7220e+07
I(0) uncertainty (real space) i0_real_error1.6120e+06
Rg (reciprocal space) rg_reciprocal31.79
I(0) (reciprocal space) i0_reciprocal97220000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32870000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5affA01
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)