9ymw

De novo initial transcribing RNA polymerase with 5-mer RNA CCAUC (RPitc5a)

Method: ELECTRON MICROSCOPY Dmax: 177.2 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit beta

Escherichia coli

UniProt P0A8V2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain I; UniProt 1–1342 Not recorded DNA-directed RNA polymerase subunit omega × 1 (P0A800) Nascent RNA × 1 T7A1 promoter fragment non-template strand × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) RNA polymerase sigma factor RpoD × 1 (P00579) T7A1 promoter fragment template strand × 1 POP PYROPHOSPHATE 2- × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

219 other PDB entries and 240 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain I; PDBConstruct 1–1342; UniProt 1–1342

DNA-directed RNA polymerase subunit omega

Escherichia coli

UniProt P0A800

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain K; UniProt 1–91 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) Nascent RNA × 1 T7A1 promoter fragment non-template strand × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) RNA polymerase sigma factor RpoD × 1 (P00579) T7A1 promoter fragment template strand × 1 POP PYROPHOSPHATE 2- × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

258 other PDB entries and 277 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–91; UniProt 1–91

DNA-directed RNA polymerase subunit alpha

Escherichia coli

UniProt P0A7Z4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain G; UniProt 1–329 Chain H; UniProt 1–329 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Nascent RNA × 1 T7A1 promoter fragment non-template strand × 1 ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) RNA polymerase sigma factor RpoD × 1 (P00579) T7A1 promoter fragment template strand × 1 POP PYROPHOSPHATE 2- × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

276 other PDB entries and 305 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–329; UniProt 1–329 Author chain H; PDBConstruct 1–329; UniProt 1–329

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli

UniProt P0A8T7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain J; UniProt 1–1407 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Nascent RNA × 1 T7A1 promoter fragment non-template strand × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) RNA polymerase sigma factor RpoD × 1 (P00579) T7A1 promoter fragment template strand × 1 POP PYROPHOSPHATE 2- × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

239 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–1407; UniProt 1–1407

RNA polymerase sigma factor RpoD

Escherichia coli

UniProt P00579

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain L; UniProt 1–613 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Nascent RNA × 1 T7A1 promoter fragment non-template strand × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) T7A1 promoter fragment template strand × 1 POP PYROPHOSPHATE 2- × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

91 other PDB entries and 132 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOD_ECOLI
Isoform
PDB entities 7
Chains and sequence ranges Author chain L; PDBConstruct 4–616; UniProt 1–613

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 9ymw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ymw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ymw
Deposition date deposition_date2025-10-10
Structure title titleDe novo initial transcribing RNA polymerase with 5-mer RNA CCAUC (RPitc5a)
Keywords keywordsRNA polymerase, initial transcribing complex, nucleotide addition, promoter escape, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.13
Radius of gyration Rg (electron density) rg_electron53.46
Forward intensity I(0) i03365040000.00
Molecular weight molecular_weight454130.0 kDa
Excluded volume excluded_volume555960 ų
Envelope volume envelope_volume861210 ų
Hydration-shell volume shell_volume129080 ų
Envelope diameter envelope_diameter190.3
Shell Rg shell_rg59.97
Envelope Rg envelope_rg53.43
Shape Rg shape_rg53.45
Total Rg total_rg53.68
Total atoms total_atoms31704
Residues n_residues3812
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 dmax177.2
Rg (real space) rg_real53.99
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real3.3650e+09
I(0) uncertainty (real space) i0_real_error6.9880e+07
Rg (reciprocal space) rg_reciprocal54.24
I(0) (reciprocal space) i0_reciprocal3366000000.0000
Solution quality estimate total_estimate0.8701
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.2
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.261
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha553300000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.789

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)