SAXSdb — 8pew

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

Transcription termination factor Rho

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 34	Polarity suppression protein × 16 （P05460） PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 16 MAGNESIUM ION × 16	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0A0GPI6_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–419； UniProt 25–443 Author chain B； PDBConstruct 1–419； UniProt 25–443 Author chain C； PDBConstruct 1–419； UniProt 25–443 Author chain D； PDBConstruct 1–419； UniProt 25–443 Author chain E； PDBConstruct 1–419； UniProt 25–443 Author chain F； PDBConstruct 1–419； UniProt 25–443 Author chain G； PDBConstruct 1–419； UniProt 25–443 Author chain H； PDBConstruct 1–419； UniProt 25–443 Author chain I； PDBConstruct 1–419； UniProt 25–443 Author chain J； PDBConstruct 1–419； UniProt 25–443 Author chain K； PDBConstruct 1–419； UniProt 25–443 Author chain L； PDBConstruct 1–419； UniProt 25–443 Author chain M； PDBConstruct 1–419； UniProt 25–443 Author chain N； PDBConstruct 1–419； UniProt 25–443 Author chain O； PDBConstruct 1–419； UniProt 25–443 Author chain P； PDBConstruct 1–419； UniProt 25–443 Author chain X； PDBConstruct 1–419； UniProt 25–443 Author chain Y； PDBConstruct 1–419； UniProt 25–443

Polarity suppression protein

Enterobacteria phage P4

UniProt P05460

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 34	Transcription termination factor Rho × 18 （A0A0A0GPI6） PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 16 MAGNESIUM ION × 16	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VPSU_BPP4
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain a； PDBConstruct 1–190； UniProt 1–190 Author chain b； PDBConstruct 1–190； UniProt 1–190 Author chain c； PDBConstruct 1–190； UniProt 1–190 Author chain d； PDBConstruct 1–190； UniProt 1–190 Author chain e； PDBConstruct 1–190； UniProt 1–190 Author chain f； PDBConstruct 1–190； UniProt 1–190 Author chain g； PDBConstruct 1–190； UniProt 1–190 Author chain h； PDBConstruct 1–190； UniProt 1–190 Author chain i； PDBConstruct 1–190； UniProt 1–190 Author chain j； PDBConstruct 1–190； UniProt 1–190 Author chain k； PDBConstruct 1–190； UniProt 1–190 Author chain l； PDBConstruct 1–190； UniProt 1–190 Author chain m； PDBConstruct 1–190； UniProt 1–190 Author chain n； PDBConstruct 1–190； UniProt 1–190 Author chain o； PDBConstruct 1–190； UniProt 1–190 Author chain p； PDBConstruct 1–190； UniProt 1–190

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_id	8pew
Deposition date deposition_date	2023-06-15
Structure title title	Rho-ATPgS-Psu complex III expanded
Keywords keywords	Transcription termination, Phage inhibitor, GENE REGULATION; GENE REGULATION
Experimental Method method	ELECTRON 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.

8pew__assembly_1__model_1

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

Download this curve (.dat)

8pew__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8pew__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	82.59 Å
Rg (electron density)	82.66 Å
Total Rg	82.55 Å
Atom count	83524
Residues	10534
Excluded volume	1483800 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8pew__assembly_1__model_1`	34-meric （34）	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 (4)

Entity 1 Entity 1 polymer

Description description	Transcription termination factor Rho
Molecular weight formula_weight	47070.2 kDa
EC 编号 ec_number	3.6.4.-
Source method src_method	man
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,X,Y
Atom count atom_count	83524

MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Polarity suppression protein
Molecular weight formula_weight	21393.1 kDa
Source method src_method	man
Copy count entity_count	16

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,b,c,d,e,f,g,h,i,j,k,l,m,n,o,p

MESTALQQAFDTCQNNKAAWLQRKNELAAAEQEYLRLLSGEGRNVSRLDELRNIIEVRKWQVNQAAGRYIRSHEAVQHISIRDRLNDFMQQHGTALAAALAPELMGYSELTAIARNCAIQRATDALREALLSWLAKGEKINYSAQDSDILTTIGFRPDVASVDDSREKFTPAQNMIFSRKSAQLASRQSV

Source Source

Source organism organism	Enterobacteria phage P4
NCBI taxonomy ID ncbi_taxonomy_id	10680
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	16

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	4.30 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	15407

Rho-ATPgS-Psu complex III expanded

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

Transcription termination factor Rho

State in the Current Structure

Other States of the Same Protein in the Database

Polarity suppression protein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

8pew__assembly_1__model_1

8pew__assembly_1__model_1 | I(q)

8pew__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

7. Citations (1)

Rho-ATPgS-Psu complex III expanded

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

Transcription termination factor Rho

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Polarity suppression protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

8pew__assembly_1__model_1

8pew__assembly_1__model_1 | I(q)

8pew__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

7. Citations (1)