SAXSdb — 8z4d

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

Flagellar M-ring protein,Flagellar motor switch protein FliG

Vibrio alginolyticus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 34	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0T7EAG0_9VIBR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 595–945； UniProt 1–351 Author chain 2； PDBConstruct 595–945； UniProt 1–351 Author chain 3； PDBConstruct 595–945； UniProt 1–351 Author chain 4； PDBConstruct 595–945； UniProt 1–351 Author chain 5； PDBConstruct 595–945； UniProt 1–351 Author chain 6； PDBConstruct 595–945； UniProt 1–351 Author chain 7； PDBConstruct 595–945； UniProt 1–351 Author chain 8； PDBConstruct 595–945； UniProt 1–351 Author chain 9； PDBConstruct 595–945； UniProt 1–351 Author chain A； PDBConstruct 595–945； UniProt 1–351 Author chain B； PDBConstruct 595–945； UniProt 1–351 Author chain C； PDBConstruct 595–945； UniProt 1–351 Author chain D； PDBConstruct 595–945； UniProt 1–351 Author chain E； PDBConstruct 595–945； UniProt 1–351 Author chain F； PDBConstruct 595–945； UniProt 1–351 Author chain G； PDBConstruct 595–945； UniProt 1–351 Author chain H； PDBConstruct 595–945； UniProt 1–351 Author chain I； PDBConstruct 595–945； UniProt 1–351 Author chain J； PDBConstruct 595–945； UniProt 1–351 Author chain K； PDBConstruct 595–945； UniProt 1–351 Author chain L； PDBConstruct 595–945； UniProt 1–351 Author chain M； PDBConstruct 595–945； UniProt 1–351 Author chain N； PDBConstruct 595–945； UniProt 1–351 Author chain O； PDBConstruct 595–945； UniProt 1–351 Author chain P； PDBConstruct 595–945； UniProt 1–351 Author chain Q； PDBConstruct 595–945； UniProt 1–351 Author chain R； PDBConstruct 595–945； UniProt 1–351 Author chain S； PDBConstruct 595–945； UniProt 1–351 Author chain T； PDBConstruct 595–945； UniProt 1–351 Author chain U； PDBConstruct 595–945； UniProt 1–351 Author chain V； PDBConstruct 595–945； UniProt 1–351 Author chain W； PDBConstruct 595–945； UniProt 1–351 Author chain X； PDBConstruct 595–945； UniProt 1–351 Author chain Y； PDBConstruct 595–945； UniProt 1–351

Flagellar M-ring protein,Flagellar motor switch protein FliG

Vibrio alginolyticus

UniProt Q75N27

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 34	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q75N27_VIBAL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 17–594； UniProt 1–578 Author chain 2； PDBConstruct 17–594； UniProt 1–578 Author chain 3； PDBConstruct 17–594； UniProt 1–578 Author chain 4； PDBConstruct 17–594； UniProt 1–578 Author chain 5； PDBConstruct 17–594； UniProt 1–578 Author chain 6； PDBConstruct 17–594； UniProt 1–578 Author chain 7； PDBConstruct 17–594； UniProt 1–578 Author chain 8； PDBConstruct 17–594； UniProt 1–578 Author chain 9； PDBConstruct 17–594； UniProt 1–578 Author chain A； PDBConstruct 17–594； UniProt 1–578 Author chain B； PDBConstruct 17–594； UniProt 1–578 Author chain C； PDBConstruct 17–594； UniProt 1–578 Author chain D； PDBConstruct 17–594； UniProt 1–578 Author chain E； PDBConstruct 17–594； UniProt 1–578 Author chain F； PDBConstruct 17–594； UniProt 1–578 Author chain G； PDBConstruct 17–594； UniProt 1–578 Author chain H； PDBConstruct 17–594； UniProt 1–578 Author chain I； PDBConstruct 17–594； UniProt 1–578 Author chain J； PDBConstruct 17–594； UniProt 1–578 Author chain K； PDBConstruct 17–594； UniProt 1–578 Author chain L； PDBConstruct 17–594； UniProt 1–578 Author chain M； PDBConstruct 17–594； UniProt 1–578 Author chain N； PDBConstruct 17–594； UniProt 1–578 Author chain O； PDBConstruct 17–594； UniProt 1–578 Author chain P； PDBConstruct 17–594； UniProt 1–578 Author chain Q； PDBConstruct 17–594； UniProt 1–578 Author chain R； PDBConstruct 17–594； UniProt 1–578 Author chain S； PDBConstruct 17–594； UniProt 1–578 Author chain T； PDBConstruct 17–594； UniProt 1–578 Author chain U； PDBConstruct 17–594； UniProt 1–578 Author chain V； PDBConstruct 17–594； UniProt 1–578 Author chain W； PDBConstruct 17–594； UniProt 1–578 Author chain X； PDBConstruct 17–594； UniProt 1–578 Author chain Y； PDBConstruct 17–594； UniProt 1–578

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	8z4d
Deposition date deposition_date	2024-04-17
Structure title title	Structure of the S-ring region of the Vibrio flagellar MS-ring protein FliF with 34-fold symmetry applied
Keywords keywords	Complex, Rotor, MOTOR PROTEIN; MOTOR PROTEIN
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.

8z4d__assembly_1__model_1

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

Download this curve (.dat)

8z4d__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8z4d__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	87.16 Å
Rg (electron density)	87.88 Å
Total Rg	88.05 Å
Atom count	38862
Residues	4896
Excluded volume	683200 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8z4d__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 (1)

Entity 1 Entity 1 polymer

Description description	Flagellar M-ring protein,Flagellar motor switch protein FliG
Molecular weight formula_weight	104416.8 kDa
Mutation mutation	G214S
Source method src_method	man
Copy count entity_count	34

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,3,4,5,6,7,8,9,A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y
Atom count atom_count	38862

MNHKVHHHHHHIEGRHMADKSTDLTVTEGGSDGALVASSDVDVESQNPDLEERSASKFDMAVGDLDLLRQVVLVLSISICVALIVMLFFWVKEPEMRPLGAYETEELIPVLDYLDQQKINYKLDGNTISVESSEYNSIKLGMVRSGVNQATEAGDDILLQDMGFGVSQRLEQERLKLSRERQLAQAIEEMKQVRKARVLLALPKHSVFVRHNQEASASVFLTLSTGTNLKQQEVDSIVDMVASAVPGMKTSRITVTDQHGRLLSSGSQDPASAARRKEQELERSQEQALREKIDSVLLPILGYGNYTAQVDIQMDFSAVEQTRKRFDPNTPATRSEYALEDYNNGNMVAGIPGALSNQPPADASIPQDVAQMKDGSVMGQGSVRKESTRNFELDTTISHERKQTGTVARQTVSVAIKDRRQVNPDTGEVTYTPMSESEINAIRQVLIGTVGFDQGRGDLLNVLSVKFAEPEAEQLEEPPIWEHPNFSDWVRWFASALVIIVVVLVLVRPAMKKLLNPTSDDEDEMYGPDGLPIGADGETSLIGSDIESSELFEFGSSIDLPNLHKDEDVLKAVRALVANEPELAAQVVKNWMNDMANDIVPQDDNAAGMPVELDVSTITGEEKAAILLLSLNEQDAAGIIRHLEPKQVQRVGSAMAKAKDLSQDKVSAVHRAFLEDIQKYTNIGMGSEDFMRNALVAALGEDKANNLVDQILLGTGSKGLDSLKWMDPRQVASIIVNEHPQIQTIVLSYLEADQSAEILSQFPERVRLDLMMRIANLEEVQPSALAELNEIMEKQFAGQAGAQAAKISGLKAAAEIMNYLDNNVEGLLMEQIRDQDEDMATQIQDLMFVFENLVEVDDQGIQKLLRDVPQDVLQKALKGADDSLREKVFKNMSKRAAEMMRDDIEAMPPVRVADVEAAQKEILAIARRMADAGELMLSGGADEFL

Source Source

Source organism organism	Vibrio alginolyticus
NCBI taxonomy ID ncbi_taxonomy_id	663
Host organism host_organism	Escherichia coli BL21(DE3)

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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	—

Resolution resolution	3.33 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	43546

Structure of the S-ring region of the Vibrio flagellar MS-ring protein FliF with 34-fold symmetry applied

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

Flagellar M-ring protein,Flagellar motor switch protein FliG

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar M-ring protein,Flagellar motor switch protein FliG

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

8z4d__assembly_1__model_1

8z4d__assembly_1__model_1 | I(q)

8z4d__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (1)

Structure of the S-ring region of the Vibrio flagellar MS-ring protein FliF with 34-fold symmetry applied

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

Flagellar M-ring protein,Flagellar motor switch protein FliG

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Flagellar M-ring protein,Flagellar motor switch protein FliG

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

8z4d__assembly_1__model_1

8z4d__assembly_1__model_1 | I(q)

8z4d__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (1)