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9m67

the flagellar filament cap FliD in complex with FliC

Method: ELECTRON MICROSCOPY Dmax: 190.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Flagellin,Flagellar hook-associated protein 2

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt P06179

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count Chain A； UniProt 1–495 Chain B； UniProt 1–495 Chain C； UniProt 1–495 Chain D； UniProt 1–495 Chain E； UniProt 1–495 Chain F； UniProt 1–495 Chain G； UniProt 1–495 Chain H； UniProt 1–495 Chain I； UniProt 1–495 Chain J； UniProt 1–495 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.40 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 9M67 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1IO1 CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN Deposited 2000-12-28 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 53–450（398 aa） Fragment：F41 L-TYPE (RESIDUES 54-451)
Mutation：G426A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；289 K；PEG 6000, NaCl, Glycerol, Iso-Propanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 2.00 Å R-free 0.266
1UCU R-type straight flagellar filament made of full-length flagellin Deposited 2003-04-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–494（494 aa）
Mutation：A449V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL；pH 7.8；150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL
Resolution 4.00 Å
3A5X L-type straight flagellar filament made of full-length flagellin Deposited 2009-08-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–495（494 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL；pH 7.8；150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
5YUD Flagellin derivative in complex with the NLR protein NAIP5 Deposited 2017-11-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 452–495（44 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.28 Å
6CH3 Crystal structure of the cytoplasmic domain of FlhA and FliS-FliC complex Deposited 2018-02-21 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 455–495（41 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；tascimate
Resolution 2.68 Å R-free 0.258
8FML Cryo-EM structure of NLR family apoptosis inhibitory protein 5 (NAIP5) in complex with a full-length flagellin (FliC) ligand Deposited 2022-12-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–495（495 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.93 Å
9IWQ Salmonella enterica serovar Typhimurium FliC(G426A)delta(204-292) forming the L-type straight filament Deposited 2024-07-25 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–495（494 aa）
Mutation：G426A No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.08 Å
9M5T Structure of the flagellar filament in short-length at 3.02 angstroms resolution Deposited 2025-03-06 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 44 PDB declaration: 44-meric
Chain AA 1–495（495 aa）
Chain AB 1–495（495 aa）
Chain AC 1–495（495 aa）
Chain AD 1–495（495 aa）
Chain AE 1–495（495 aa）
Chain AF 1–495（495 aa）
Chain AG 1–495（495 aa）
Chain AH 1–495（495 aa）
Chain AI 1–495（495 aa）
Chain AJ 1–495（495 aa）
Chain AK 1–495（495 aa）
Chain BA 1–495（495 aa）
Chain BB 1–495（495 aa）
Chain BC 1–495（495 aa）
Chain BD 1–495（495 aa）
Chain BE 1–495（495 aa）
Chain BF 1–495（495 aa）
Chain BG 1–495（495 aa）
Chain BH 1–495（495 aa）
Chain BI 1–495（495 aa）
Chain BJ 1–495（495 aa）
Chain BK 1–495（495 aa）
Chain CA 1–495（495 aa）
Chain CB 1–495（495 aa）
Chain CC 1–495（495 aa）
Chain CD 1–495（495 aa）
Chain CE 1–495（495 aa）
Chain CF 1–495（495 aa）
Chain CG 1–495（495 aa）
Chain CH 1–495（495 aa）
Chain CI 1–495（495 aa）
Chain CJ 1–495（495 aa）
Chain CK 1–495（495 aa）
Chain DA 1–495（495 aa）
Chain DB 1–495（495 aa）
Chain DC 1–495（495 aa）
Chain DD 1–495（495 aa）
Chain DE 1–495（495 aa）
Chain DF 1–495（495 aa）
Chain DG 1–495（495 aa）
Chain DH 1–495（495 aa）
Chain DI 1–495（495 aa）
Chain DJ 1–495（495 aa）
Chain DK 1–495（495 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.02 Å
9M6H structure of FliD-FliC at a 10:10 stoichiometry Deposited 2025-03-07 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain B 54–454（401 aa）
Chain D 54–454（401 aa）
Chain F 54–454（401 aa）
Chain H 54–454（401 aa）
Chain J 54–454（401 aa）
Chain L 54–454（401 aa）
Chain N 54–454（401 aa）
Chain P 54–454（401 aa）
Chain R 54–454（401 aa）
Chain T 54–454（401 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.27 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIC_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 21–515； UniProt 1–495 Author chain B； PDBConstruct 21–515； UniProt 1–495 Author chain C； PDBConstruct 21–515； UniProt 1–495 Author chain D； PDBConstruct 21–515； UniProt 1–495 Author chain E； PDBConstruct 21–515； UniProt 1–495 Author chain F； PDBConstruct 21–515； UniProt 1–495 Author chain G； PDBConstruct 21–515； UniProt 1–495 Author chain H； PDBConstruct 21–515； UniProt 1–495 Author chain I； PDBConstruct 21–515； UniProt 1–495 Author chain J； PDBConstruct 21–515； UniProt 1–495

Flagellin,Flagellar hook-associated protein 2

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt P16328

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count Chain A； UniProt 1–467 Chain B； UniProt 1–467 Chain C； UniProt 1–467 Chain D； UniProt 1–467 Chain E； UniProt 1–467 Chain F； UniProt 1–467 Chain G； UniProt 1–467 Chain H； UniProt 1–467 Chain I； UniProt 1–467 Chain J； UniProt 1–467 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.40 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 9M67 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5GNA Crystal Structure of flagellin assembly related protein Deposited 2016-07-20 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 401–467（67 aa） Fragment：UNP RESIDUES 401-467
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；296 K；5% PEG 400, 10% isopropanol, 0.2 M magnesium chloride, 0.1 M Tris-HCl pH 8.0
Resolution 2.30 Å R-free 0.229
5KRW Recognition and targeting mechanisms by chaperones in flagella assembly and operation Deposited 2016-07-07 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 428–467（40 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；305 K；Ionic strength (raw mmCIF value) 120；Pressure 1
NMR sample composition 1 mM [U-99% 13C; U-99% 15N; U-99% 2H] FliT-FliD_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.5 mM EDTA, 5 mM beta-mercaptoethanol, 0.05 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM U[15N,2H] 1H-13C-ILVMAT-methyl FliT-FliD_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.5 mM EDTA, 5 mM beta-mercaptoethanol, 0.05 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-99% 13C; U-99% 15N] FliT-FliD_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.5 mM EDTA, 5 mM beta-mercaptoethanol, 0.05 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 428–467（40 aa） Fragment：unp residues 1-122; 428-467
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；CaCl2, PEG8000, Sodium cacodylate
Resolution 2.70 Å R-free 0.266
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 428–467（40 aa） Fragment：unp residues 1-122; 428-467
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；CaCl2, PEG8000, Sodium cacodylate
Resolution 2.70 Å R-free 0.266
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 428–467（40 aa） Fragment：unp residues 1-122; 428-467
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；CaCl2, PEG8000, Sodium cacodylate
Resolution 2.70 Å R-free 0.266
9M68 the flagellar filament cap FliD in complex with FlgL Deposited 2025-03-07 Different construct Different mutation/modification Different oligomeric state Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 19–433（415 aa）
Chain B 19–433（415 aa）
Chain D 19–433（415 aa）
Chain G 19–433（415 aa）
Chain I 19–433（415 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9M6H structure of FliD-FliC at a 10:10 stoichiometry Deposited 2025-03-07 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric
Chain A 21–450（430 aa）
Chain C 21–450（430 aa）
Chain E 21–450（430 aa）
Chain G 21–450（430 aa）
Chain I 21–450（430 aa）
Chain K 21–450（430 aa）
Chain M 21–450（430 aa）
Chain O 21–450（430 aa）
Chain Q 21–450（430 aa）
Chain S 21–450（430 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.27 Å
9M6I structure of the FliD cap Deposited 2025-03-07 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–467（467 aa）
Chain B 1–467（467 aa）
Chain C 1–467（467 aa）
Chain D 1–467（467 aa）
Chain E 1–467（467 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.06 Å
9U4R Structure of the intial complex in filament assembly at 3.23 angstroms resolution, conformation 2. Deposited 2025-03-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 73 PDB declaration: 73-meric
Chain AA 1–467（467 aa）
Chain AB 1–467（467 aa）
Chain AC 1–467（467 aa）
Chain AD 1–467（467 aa）
Chain AE 1–467（467 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.23 Å
9U7Y Structure of the tip region of the intial complex in bacterial flagellar filament assembly at 3.68 angstroms resolution, conformation 3. Deposited 2025-03-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric
Chain AA 1–467（467 aa）
Chain AB 1–467（467 aa）
Chain AC 1–467（467 aa）
Chain AD 1–467（467 aa）
Chain AE 1–467（467 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.68 Å

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLID_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 526–992； UniProt 1–467 Author chain B； PDBConstruct 526–992； UniProt 1–467 Author chain C； PDBConstruct 526–992； UniProt 1–467 Author chain D； PDBConstruct 526–992； UniProt 1–467 Author chain E； PDBConstruct 526–992； UniProt 1–467 Author chain F； PDBConstruct 526–992； UniProt 1–467 Author chain G； PDBConstruct 526–992； UniProt 1–467 Author chain H； PDBConstruct 526–992； UniProt 1–467 Author chain I； PDBConstruct 526–992； UniProt 1–467 Author chain J； PDBConstruct 526–992； UniProt 1–467

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 9m67

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m67
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m67
Deposition date deposition_date2025-03-07
Structure title titlethe flagellar filament cap FliD in complex with FliC
Keywords keywordsComplex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier61.52 Å
Radius of gyration Rg (electron density) rg_electron60.77 Å
Forward intensity I(0) i02916230000.00
Molecular weight molecular_weight436300.0 kDa
Excluded volume excluded_volume540250 ų
Envelope volume envelope_volume1044100 ų
Hydration-shell volume shell_volume142280 ų
Envelope diameter envelope_diameter198.2 Å
Shell Rg shell_rg67.74 Å
Envelope Rg envelope_rg56.64 Å
Shape Rg shape_rg60.80 Å
Total Rg total_rg60.87 Å
Total atoms total_atoms30640
Residues n_residues4150
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax190.8 Å
Rg (real space) rg_real61.07 Å
Rg uncertainty (real space) rg_real_error1.83 Å
I(0) (real space) i0_real2.9160e+09
I(0) uncertainty (real space) i0_real_error5.7880e+07
Rg (reciprocal space) rg_reciprocal61.88 Å
I(0) (reciprocal space) i0_reciprocal2920000000.0000
Solution quality estimate total_estimate0.8682
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary88.0 Å
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.1300 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha266000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.791
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)