7bof

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

Method: ELECTRON MICROSCOPY Dmax: 196.1 Å Quality: GOOD

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

30S ribosomal protein S4

OrganismNot specified

UniProt P0A7V8

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–206 Not recorded 16S rRNA × 1 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

458 other PDB entries and 503 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS4_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–206; UniProt 1–206

30S ribosomal protein S5

OrganismNot specified

UniProt P0A7W1

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 1–167 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

483 other PDB entries and 529 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS5_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–167; UniProt 1–167

30S ribosomal protein S6

OrganismNot specified

UniProt P02358

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain F; UniProt 1–135 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

517 other PDB entries and 562 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS6_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–135; UniProt 1–135

30S ribosomal protein S8

OrganismNot specified

UniProt P0A7W7

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain H; UniProt 1–130 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

390 other PDB entries and 437 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS8_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 1–130; UniProt 1–130

30S ribosomal protein S11

OrganismNot specified

UniProt P0A7R9

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 1–129 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

412 other PDB entries and 457 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS11_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain K; PDBConstruct 1–129; UniProt 1–129

30S ribosomal protein S12

OrganismNot specified

UniProt P0A7S3

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain L; UniProt 1–124 Non-standard monomer:Yes (specific site not provided by mmCIF) 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

428 other PDB entries and 474 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS12_ECOLI
Isoform
PDB entities 7
Chains and sequence ranges Author chain L; PDBConstruct 1–124; UniProt 1–124

30S ribosomal protein S15

OrganismNot specified

UniProt P0ADZ4

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain O; UniProt 1–89 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

378 other PDB entries and 418 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS15_ECOLI
Isoform
PDB entities 8
Chains and sequence ranges Author chain O; PDBConstruct 1–89; UniProt 1–89

30S ribosomal protein S16

OrganismNot specified

UniProt P0A7T3

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain P; UniProt 1–82 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

391 other PDB entries and 437 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS16_ECOLI
Isoform
PDB entities 9
Chains and sequence ranges Author chain P; PDBConstruct 1–82; UniProt 1–82

30S ribosomal protein S17

OrganismNot specified

UniProt P0AG63

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain Q; UniProt 1–84 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S18 × 1 (P0A7T7) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

400 other PDB entries and 443 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS17_ECOLI
Isoform
PDB entities 10
Chains and sequence ranges Author chain Q; PDBConstruct 1–84; UniProt 1–84

30S ribosomal protein S18

OrganismNot specified

UniProt P0A7T7

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain R; UniProt 1–75 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S20 × 1 (P0A7U7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

388 other PDB entries and 434 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS18_ECOLI
Isoform
PDB entities 11
Chains and sequence ranges Author chain R; PDBConstruct 1–75; UniProt 1–75

30S ribosomal protein S20

OrganismNot specified

UniProt P0A7U7

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 × 11 RNA 1 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain T; UniProt 1–87 Not recorded 16S rRNA × 1 30S ribosomal protein S4 × 1 (P0A7V8) 30S ribosomal protein S5 × 1 (P0A7W1) 30S ribosomal protein S6 × 1 (P02358) 30S ribosomal protein S8 × 1 (P0A7W7) 30S ribosomal protein S11 × 1 (P0A7R9) 30S ribosomal protein S12 × 1 (P0A7S3) 30S ribosomal protein S15 × 1 (P0ADZ4) 30S ribosomal protein S16 × 1 (P0A7T3) 30S ribosomal protein S17 × 1 (P0AG63) 30S ribosomal protein S18 × 1 (P0A7T7) MG MAGNESIUM ION × 129 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 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.

394 other PDB entries and 439 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS20_ECOLI
Isoform
PDB entities 12
Chains and sequence ranges Author chain T; PDBConstruct 1–87; UniProt 1–87

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 7bof

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bof
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7bof
Deposition date deposition_date2021-01-25
Structure title titleBacterial 30S ribosomal subunit assembly complex state I (body 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_guinier55.56
Radius of gyration Rg (electron density) rg_electron56.07
Forward intensity I(0) i08163280000.00
Molecular weight molecular_weight489560.0 kDa
Excluded volume excluded_volume499730 ų
Envelope volume envelope_volume807310 ų
Hydration-shell volume shell_volume119900 ų
Envelope diameter envelope_diameter214.9
Shell Rg shell_rg58.98
Envelope Rg envelope_rg55.44
Shape Rg shape_rg56.09
Total Rg total_rg56.08
Total atoms total_atoms32814
Residues n_residues2302
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 dmax196.1
Rg (real space) rg_real55.67
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real8.1630e+09
I(0) uncertainty (real space) i0_real_error1.7450e+08
Rg (reciprocal space) rg_reciprocal55.45
I(0) (reciprocal space) i0_reciprocal8161000000.0000
Solution quality estimate total_estimate0.8530
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.0
Skewness Skewness skewness0.465
Kurtosis Kurtosis kurtosis-0.116
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha788000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.751; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.834

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7bofD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1050 — Ribosomal Protein S4 Delta 41; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Ribosomal protein S4/S9, N-terminal domain
Domain ID domain_id7bofD02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology290 — Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A
Homologous superfamily homologous superfamily10 — RNA-binding S4 domain
Domain ID domain_id7bofE01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily20
Domain ID domain_id7bofE02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)