SAXSdb — 9yee

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

Flagellar basal-body rod protein FlgG

OrganismNot specified

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 heterocomplex Heteromer Protein × 49 PDB declaration: 49-meric（49） Consistent with protein copy count	Chain Ba； UniProt 1–262 Chain Bb； UniProt 1–262 Chain Bc； UniProt 1–262 Chain Bd； UniProt 1–262 Chain Be； UniProt 1–262 Chain Bf； UniProt 1–262 Chain Bg； UniProt 1–262 Chain Bh； UniProt 1–262 Chain Bi； UniProt 1–262 Chain Bj； UniProt 1–262 Chain Bk； UniProt 1–262 Chain Bl； UniProt 1–262 Chain Bm； UniProt 1–262 Chain Bn； UniProt 1–262 Chain Bo； UniProt 1–262 Chain Bp； UniProt 1–262 Chain Bq； UniProt 1–262 Chain Br； UniProt 1–262 Chain Bs； UniProt 1–262 Chain Bt； UniProt 1–262 Chain Bu； UniProt 1–262 Chain Bv； UniProt 1–262 Chain Bw； UniProt 1–262 Chain Bx； UniProt 1–262 Chain By； UniProt 1–262 Chain Bz； UniProt 1–262 Chain Cb； UniProt 1–262	Not recorded	Flagellar basal-body rod protein FlgF × 5 （Q9KQ11） Flagellar hook protein FlgE × 17 （Q9KQ10）	ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions	Resolution 3.44 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.

Other PDB	Difference from Current Entry 9YEE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YH6 Composite structure of the sheathed flagellar motor in Vibrio cholerae adopting a lower FOMC conformation Deposited 2025-09-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 407 PDB declaration: 407-meric	Chain Aa 1–262（262 aa） Chain Ab 1–262（262 aa） Chain Ac 1–262（262 aa） Chain Ad 1–262（262 aa） Chain Ae 1–262（262 aa） Chain Af 1–262（262 aa） Chain Ag 1–262（262 aa） Chain Ah 1–262（262 aa） Chain Ai 1–262（262 aa） Chain Aj 1–262（262 aa） Chain Ak 1–262（262 aa） Chain Al 1–262（262 aa） Chain Am 1–262（262 aa） Chain An 1–262（262 aa） Chain Ao 1–262（262 aa） Chain Ap 1–262（262 aa） Chain Aq 1–262（262 aa） Chain Ar 1–262（262 aa） Chain As 1–262（262 aa） Chain At 1–262（262 aa） Chain Au 1–262（262 aa） Chain Av 1–262（262 aa） Chain Aw 1–262（262 aa） Chain Ax 1–262（262 aa） Chain Ay 1–262（262 aa） Chain Az 1–262（262 aa） Chain Bb 1–262（262 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.60 Å
9YH7 Composite structure of the sheathed flagellar motor in Vibrio cholerae adopting a higher FOMC conformation Deposited 2025-09-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 407 PDB declaration: 407-meric	Chain Aa 1–262（262 aa） Chain Ab 1–262（262 aa） Chain Ac 1–262（262 aa） Chain Ad 1–262（262 aa） Chain Ae 1–262（262 aa） Chain Af 1–262（262 aa） Chain Ag 1–262（262 aa） Chain Ah 1–262（262 aa） Chain Ai 1–262（262 aa） Chain Aj 1–262（262 aa） Chain Ak 1–262（262 aa） Chain Al 1–262（262 aa） Chain Am 1–262（262 aa） Chain An 1–262（262 aa） Chain Ao 1–262（262 aa） Chain Ap 1–262（262 aa） Chain Aq 1–262（262 aa） Chain Ar 1–262（262 aa） Chain As 1–262（262 aa） Chain At 1–262（262 aa） Chain Au 1–262（262 aa） Chain Av 1–262（262 aa） Chain Aw 1–262（262 aa） Chain Ax 1–262（262 aa） Chain Ay 1–262（262 aa） Chain Az 1–262（262 aa） Chain Bb 1–262（262 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.60 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q9KQ12_VIBCH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain Ba； PDBConstruct 1–262； UniProt 1–262 Author chain Bb； PDBConstruct 1–262； UniProt 1–262 Author chain Bc； PDBConstruct 1–262； UniProt 1–262 Author chain Bd； PDBConstruct 1–262； UniProt 1–262 Author chain Be； PDBConstruct 1–262； UniProt 1–262 Author chain Bf； PDBConstruct 1–262； UniProt 1–262 Author chain Bg； PDBConstruct 1–262； UniProt 1–262 Author chain Bh； PDBConstruct 1–262； UniProt 1–262 Author chain Bi； PDBConstruct 1–262； UniProt 1–262 Author chain Bj； PDBConstruct 1–262； UniProt 1–262 Author chain Bk； PDBConstruct 1–262； UniProt 1–262 Author chain Bl； PDBConstruct 1–262； UniProt 1–262 Author chain Bm； PDBConstruct 1–262； UniProt 1–262 Author chain Bn； PDBConstruct 1–262； UniProt 1–262 Author chain Bo； PDBConstruct 1–262； UniProt 1–262 Author chain Bp； PDBConstruct 1–262； UniProt 1–262 Author chain Bq； PDBConstruct 1–262； UniProt 1–262 Author chain Br； PDBConstruct 1–262； UniProt 1–262 Author chain Bs； PDBConstruct 1–262； UniProt 1–262 Author chain Bt； PDBConstruct 1–262； UniProt 1–262 Author chain Bu； PDBConstruct 1–262； UniProt 1–262 Author chain Bv； PDBConstruct 1–262； UniProt 1–262 Author chain Bw； PDBConstruct 1–262； UniProt 1–262 Author chain Bx； PDBConstruct 1–262； UniProt 1–262 Author chain By； PDBConstruct 1–262； UniProt 1–262 Author chain Bz； PDBConstruct 1–262； UniProt 1–262 Author chain Cb； PDBConstruct 1–262； UniProt 1–262

Flagellar basal-body rod protein FlgF

OrganismNot specified

UniProt Q9KQ11

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 heterocomplex Heteromer Protein × 49 PDB declaration: 49-meric（49） Consistent with protein copy count	Chain Ca； UniProt 1–249 Chain Cc； UniProt 1–249 Chain Cd； UniProt 1–249 Chain Cv； UniProt 1–249 Chain Cw； UniProt 1–249	Not recorded	Flagellar basal-body rod protein FlgG × 27 （Q9KQ12） Flagellar hook protein FlgE × 17 （Q9KQ10）	ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions	Resolution 3.44 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.

Other PDB	Difference from Current Entry 9YEE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YH6 Composite structure of the sheathed flagellar motor in Vibrio cholerae adopting a lower FOMC conformation Deposited 2025-09-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 407 PDB declaration: 407-meric	Chain Ba 1–249（249 aa） Chain Bc 1–249（249 aa） Chain Bd 1–249（249 aa） Chain Bv 1–249（249 aa） Chain Bw 1–249（249 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.60 Å
9YH7 Composite structure of the sheathed flagellar motor in Vibrio cholerae adopting a higher FOMC conformation Deposited 2025-09-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 407 PDB declaration: 407-meric	Chain Ba 1–249（249 aa） Chain Bc 1–249（249 aa） Chain Bd 1–249（249 aa） Chain Bv 1–249（249 aa） Chain Bw 1–249（249 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.60 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q9KQ11_VIBCH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain Ca； PDBConstruct 1–249； UniProt 1–249 Author chain Cc； PDBConstruct 1–249； UniProt 1–249 Author chain Cd； PDBConstruct 1–249； UniProt 1–249 Author chain Cv； PDBConstruct 1–249； UniProt 1–249 Author chain Cw； PDBConstruct 1–249； UniProt 1–249

Flagellar hook protein FlgE

OrganismNot specified

UniProt Q9KQ10

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 heterocomplex Heteromer Protein × 49 PDB declaration: 49-meric（49） Consistent with protein copy count	Chain Ce； UniProt 1–434 Chain Cf； UniProt 1–434 Chain Cg； UniProt 1–434 Chain Ch； UniProt 1–434 Chain Ci； UniProt 1–434 Chain Cj； UniProt 1–434 Chain Ck； UniProt 1–434 Chain Cl； UniProt 1–434 Chain Cm； UniProt 1–434 Chain Cn； UniProt 1–434 Chain Co； UniProt 1–434 Chain Cp； UniProt 1–434 Chain Cq； UniProt 1–434 Chain Cr； UniProt 1–434 Chain Cs； UniProt 1–434 Chain Ct； UniProt 1–434 Chain Cu； UniProt 1–434	Not recorded	Flagellar basal-body rod protein FlgG × 27 （Q9KQ12） Flagellar basal-body rod protein FlgF × 5 （Q9KQ11）	ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions	Resolution 3.44 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.

Other PDB	Difference from Current Entry 9YEE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YH6 Composite structure of the sheathed flagellar motor in Vibrio cholerae adopting a lower FOMC conformation Deposited 2025-09-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 407 PDB declaration: 407-meric	Chain Be 1–434（434 aa） Chain Bf 1–434（434 aa） Chain Bg 1–434（434 aa） Chain Bh 1–434（434 aa） Chain Bi 1–434（434 aa） Chain Bj 1–434（434 aa） Chain Bk 1–434（434 aa） Chain Bl 1–434（434 aa） Chain Bm 1–434（434 aa） Chain Bn 1–434（434 aa） Chain Bo 1–434（434 aa） Chain Bp 1–434（434 aa） Chain Bq 1–434（434 aa） Chain Br 1–434（434 aa） Chain Bs 1–434（434 aa） Chain Bt 1–434（434 aa） Chain Bu 1–434（434 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q9KQ10_VIBCH
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain Ce； PDBConstruct 1–434； UniProt 1–434 Author chain Cf； PDBConstruct 1–434； UniProt 1–434 Author chain Cg； PDBConstruct 1–434； UniProt 1–434 Author chain Ch； PDBConstruct 1–434； UniProt 1–434 Author chain Ci； PDBConstruct 1–434； UniProt 1–434 Author chain Cj； PDBConstruct 1–434； UniProt 1–434 Author chain Ck； PDBConstruct 1–434； UniProt 1–434 Author chain Cl； PDBConstruct 1–434； UniProt 1–434 Author chain Cm； PDBConstruct 1–434； UniProt 1–434 Author chain Cn； PDBConstruct 1–434； UniProt 1–434 Author chain Co； PDBConstruct 1–434； UniProt 1–434 Author chain Cp； PDBConstruct 1–434； UniProt 1–434 Author chain Cq； PDBConstruct 1–434； UniProt 1–434 Author chain Cr； PDBConstruct 1–434； UniProt 1–434 Author chain Cs； PDBConstruct 1–434； UniProt 1–434 Author chain Ct； PDBConstruct 1–434； UniProt 1–434 Author chain Cu； PDBConstruct 1–434； UniProt 1–434

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	9yee
Deposition date deposition_date	2025-09-24
Structure title title	Rod-hook protein in Vibrio cholerae at assembled, opened state
Keywords keywords	In situ cryo-EM, sheathed flagellar motor, Vibrio cholerae, rod-hook, assembled state, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	74.52 Å
Radius of gyration Rg (electron density) rg_electron	74.82 Å
Forward intensity I(0) i0	27982200000.00
Molecular weight molecular_weight	1375000.0 kDa
Excluded volume excluded_volume	1700600 Å³
Envelope volume envelope_volume	2327700 Å³
Hydration-shell volume shell_volume	244830 Å³
Envelope diameter envelope_diameter	297.3 Å
Shell Rg shell_rg	81.67 Å
Envelope Rg envelope_rg	76.60 Å
Shape Rg shape_rg	74.85 Å
Total Rg total_rg	74.78 Å
Total atoms total_atoms	96589
Residues n_residues	12773
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	221.8 Å
Rg (real space) rg_real	73.30 Å
Rg uncertainty (real space) rg_real_error	0.81 Å
I(0) (real space) i0_real	2.7610e+10
I(0) uncertainty (real space) i0_real_error	5.1620e+08
Rg (reciprocal space) rg_reciprocal	73.80 Å
I(0) (reciprocal space) i0_reciprocal	27930000000.0000
Solution quality estimate total_estimate	0.8344
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	84.5 Å
Skewness Skewness skewness	0.474
Kurtosis Kurtosis kurtosis	-0.196
Angular range angular_range	— – 0.1050 Å⁻¹
Current regularization parameter α current_alpha	0.1840
Highest regularization parameter α highest_alpha	4384000000.0000
Real-space data points n_real_points	22
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.901; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.093

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Flagellar basal-body rod protein FlgG
Molecular weight formula_weight	28114.3 kDa
Source method src_method	nat
Copy count entity_count	27

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Ba,Bb,Bc,Bd,Be,Bf,Bg,Bh,Bi,Bj,Bk,Bl,Bm,Bn,Bo,Bp,Bq,Br,Bs,Bt,Bu,Bv,Bw,Bx,By,Bz,Cb
Atom count atom_count	96589

MQPALWVSKTGLDAQQTNIATISNNLANASTIGFKKGRAVFEDLFYQNINQPGAQSSQNTRLPSGLMLGAGSKVVATQKVHTNGNVQTTSNSLDMMIEGDGFFQILMPDGNIAYSRNGQFTLDDEGAIVTSGAGYRLQPEIIIPEDAISITIGNDGEVSVRVRGQQDNQVLGQITTVDFINPGGLEPVGQNLYLPTGASGEPQEGVPGLDGLGDIRQSMLETSNVNVTEELVNMIEAQRVYEMNSKVISAVDKMMSFVNQQL

Entity 2 Entity 2 polymer

Description description	Flagellar basal-body rod protein FlgF
Molecular weight formula_weight	26778.3 kDa
Source method src_method	nat
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Ca,Cc,Cd,Cv,Cw

MDRALFLAMSGAKQNMQAMQLRANNLANVSTTGFRADLAQARSMQAYGEGLPSRVFSMTERPGHNFAQGSVITTGRDLDITIQGDGWISVLDKTGKEGLTRNGNLRIDETGLLLNGNGHPVLGETGAPITLPVPLNKVEIGGDGTISVRPQGAPADAMEVVDRIKLVRLNDQSLFKDVNGLFRATDPNTQFEADASVKILTGALEGSNVNAIGEMTSLIDLQRQFEMQVKMMSTAEEMDKASDSLLRSS

Entity 3 Entity 3 polymer

Description description	Flagellar hook protein FlgE
Molecular weight formula_weight	46880.3 kDa
Source method src_method	nat
Copy count entity_count	17

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Ce,Cf,Cg,Ch,Ci,Cj,Ck,Cl,Cm,Cn,Co,Cp,Cq,Cr,Cs,Ct,Cu

MSYVSLSGLSAAQMDLNTTSNNIANANTFGFKESRAEFGDVYSTSLFTNAKTTPGQGVQAAKVAQQFHEGSSIYTNNPLDLRIAGTGFFAVAKDRLVPQQNELTRNGAFHLDKNSFMVTANDEFLLGYEVNPDTGDVLSYEPKPINIPPQFGKPKQTANIDLGANLPANGDLKDPALFDITDPETYNRTTSSTIYDSMGQPYKLTTYYLKDMNQANTWQTYYTVTDKTGEKPINVVGGDAASPTGHVGHTMRFNNDGTLSSLNNGQPIVTEPLGGGANPVDLNGADVNQTLSFSLDSATQFAAPFELTKFDQDGATTGFLTKIDFDENGSVLATYSNGINTTLGRVALVRVANEQGLDKKGGTQWDATQFSGAKIWGESNKGSFGSISNGSLEQSNIDMTQELVDLISAQRNFQANSRALEVHNGLQQNILQIR

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8. Citations (1)

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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	3.44 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	77446

fit	/app/data/saxs_computation/ye/9yee/9yee.fit
pddf	/app/data/pr_computation/ye/9yee/9yee.pr.out
profile	/app/data/saxs_computation/ye/9yee/9yee.dat

Rod-hook protein in Vibrio cholerae at assembled, opened state

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

Flagellar basal-body rod protein FlgG

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar basal-body rod protein FlgF

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar hook protein FlgE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)