8q3p

Bacterial transcription termination factor Rho G150D mutant bound to ADP; C-terminal 8xHis-tag

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Transcription termination factor Rho

Escherichia

UniProt P0AG30

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 18 ADENOSINE-5'-DIPHOSPHATE × 18 MAGNESIUM ION × 18 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RHO_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 4–422; UniProt 1–419 Author chain b; PDBConstruct 4–422; UniProt 1–419 Author chain c; PDBConstruct 4–422; UniProt 1–419 Author chain d; PDBConstruct 4–422; UniProt 1–419 Author chain e; PDBConstruct 4–422; UniProt 1–419 Author chain f; PDBConstruct 4–422; UniProt 1–419 Author chain g; PDBConstruct 4–422; UniProt 1–419 Author chain h; PDBConstruct 4–422; UniProt 1–419 Author chain i; PDBConstruct 4–422; UniProt 1–419 Author chain j; PDBConstruct 4–422; UniProt 1–419 Author chain k; PDBConstruct 4–422; UniProt 1–419 Author chain l; PDBConstruct 4–422; UniProt 1–419 Author chain m; PDBConstruct 4–422; UniProt 1–419 Author chain n; PDBConstruct 4–422; UniProt 1–419 Author chain o; PDBConstruct 4–422; UniProt 1–419 Author chain p; PDBConstruct 4–422; UniProt 1–419 Author chain q; PDBConstruct 4–422; UniProt 1–419 Author chain r; PDBConstruct 4–422; 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q3p
Deposition date deposition_date2023-08-04
Structure title titleBacterial transcription termination factor Rho G150D mutant bound to ADP; C-terminal 8xHis-tag
Keywords keywordsRho, termination, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8q3p__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8q3p__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8q3p__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)71.98 Å
Rg (electron density)72.06 Å
Total Rg72.08 Å
Atom count59922
Residues7542
Excluded volume1069400 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8q3p__assembly_1__model_1 18-meric (18) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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7. Citations (1)