9gcu

Rho-P167L-ATP gamma S

Method: ELECTRON MICROSCOPY Dmax: 148.3 Å Quality: GOOD

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

Transcription termination factor Rho

Escherichia coli

UniProt P0AG30

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–419 Chain B; UniProt 1–419 Chain C; UniProt 1–419 Chain D; UniProt 1–419 Chain E; UniProt 1–419 Chain F; UniProt 1–419 Not recorded MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHO_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–419; UniProt 1–419 Author chain B; PDBConstruct 1–419; UniProt 1–419 Author chain C; PDBConstruct 1–419; UniProt 1–419 Author chain D; PDBConstruct 1–419; UniProt 1–419 Author chain E; PDBConstruct 1–419; UniProt 1–419 Author chain F; PDBConstruct 1–419; UniProt 1–419

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 9gcu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gcu
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9gcu
Deposition date deposition_date2024-08-02
Structure title titleRho-P167L-ATP gamma S
Keywords keywordsTranscription termination, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.09
Radius of gyration Rg (electron density) rg_electron46.43
Forward intensity I(0) i01172290000.00
Molecular weight molecular_weight283750.0 kDa
Excluded volume excluded_volume355390 ų
Envelope volume envelope_volume491080 ų
Hydration-shell volume shell_volume84110 ų
Envelope diameter envelope_diameter151.3
Shell Rg shell_rg55.22
Envelope Rg envelope_rg45.21
Shape Rg shape_rg46.42
Total Rg total_rg46.75
Total atoms total_atoms19892
Residues n_residues2508
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 dmax148.3
Rg (real space) rg_real46.81
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real1.1720e+09
I(0) uncertainty (real space) i0_real_error2.0830e+07
Rg (reciprocal space) rg_reciprocal47.09
I(0) (reciprocal space) i0_reciprocal1173000000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.9
Skewness Skewness skewness0.062
Kurtosis Kurtosis kurtosis-0.654
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha132300000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)