7af5

Bacterial 30S ribosomal subunit assembly complex state I (head domain)

Method: ELECTRON MICROSCOPY Dmax: 147.5 Å Quality: GOOD

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

30S ribosomal protein S2

Escherichia coli

UniProt C3TPN2

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain B; UniProt 1–241 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S14 × 1 (C3SR07) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

104 other PDB entries and 104 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3TPN2_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–241; UniProt 1–241

30S ribosomal protein S3

Escherichia coli

UniProt C3SQX2

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain C; UniProt 1–233 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S14 × 1 (C3SR07) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

36 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SQX2_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–233; UniProt 1–233

30S ribosomal protein S7

Escherichia coli

UniProt A0A5Q2GFB5

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain G; UniProt 1–179 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S14 × 1 (C3SR07) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5Q2GFB5_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–179; UniProt 1–179

30S ribosomal protein S9

Escherichia coli

UniProt C3SRY2

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain I; UniProt 1–130 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S14 × 1 (C3SR07) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

76 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SRY2_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–130; UniProt 1–130

30S ribosomal protein S10

Escherichia coli

UniProt C3SQT7

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain J; UniProt 1–103 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S14 × 1 (C3SR07) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

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

View Construct and Data Evidence
UniProt name C3SQT7_ECOLX
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–103; UniProt 1–103

30S ribosomal protein S13

Escherichia coli

UniProt C3SR52

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain M; UniProt 1–118 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S14 × 1 (C3SR07) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

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

View Construct and Data Evidence
UniProt name C3SR52_ECOLX
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–118; UniProt 1–118

30S ribosomal protein S14

Escherichia coli

UniProt C3SR07

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain N; UniProt 1–101 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S19 × 1 (C3SQW2) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SR07_ECOLX
Isoform
PDB entities 8
Chains and sequence ranges Author chain N; PDBConstruct 1–101; UniProt 1–101

30S ribosomal protein S19

Escherichia coli

UniProt C3SQW2

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–RNA Heteromer Protein × 8 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain S; UniProt 1–92 Not recorded 16SrRNA (head domain of the 30S ribosome) × 1 30S ribosomal protein S2 × 1 (C3TPN2) 30S ribosomal protein S3 × 1 (C3SQX2) 30S ribosomal protein S7 × 1 (A0A5Q2GFB5) 30S ribosomal protein S9 × 1 (C3SRY2) 30S ribosomal protein S10 × 1 (C3SQT7) 30S ribosomal protein S13 × 1 (C3SR52) 30S ribosomal protein S14 × 1 (C3SR07) MG MAGNESIUM ION × 52 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 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.

52 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SQW2_ECOLX
Isoform
PDB entities 9
Chains and sequence ranges Author chain S; PDBConstruct 1–92; UniProt 1–92

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 7af5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7af5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7af5
Deposition date deposition_date2020-09-19
Structure title titleBacterial 30S ribosomal subunit assembly complex state I (head domain)
Keywords keywordsCryo-EM, 30S biogenesis, ribosome assembly, RbfA, RsgA, YjeQ, RimP, KsgA, RsmA, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.51
Radius of gyration Rg (electron density) rg_electron42.64
Forward intensity I(0) i02172820000.00
Molecular weight molecular_weight273260.0 kDa
Excluded volume excluded_volume294750 ų
Envelope volume envelope_volume431060 ų
Hydration-shell volume shell_volume82413 ų
Envelope diameter envelope_diameter158.5
Shell Rg shell_rg48.99
Envelope Rg envelope_rg42.87
Shape Rg shape_rg42.69
Total Rg total_rg42.72
Total atoms total_atoms18531
Residues n_residues1557
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 dmax147.5
Rg (real space) rg_real41.49
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real2.1730e+09
I(0) uncertainty (real space) i0_real_error4.1860e+07
Rg (reciprocal space) rg_reciprocal41.51
I(0) (reciprocal space) i0_reciprocal2173000000.0000
Solution quality estimate total_estimate0.8445
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.5
Skewness Skewness skewness0.413
Kurtosis Kurtosis kurtosis-0.029
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha202100000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.690; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.908

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)