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6ai3

Structure of the 328-692 fragment of FlhA (T490M)

Method: X-RAY DIFFRACTION Dmax: 104.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Flagellar biosynthesis protein FlhA

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

UniProt P40729

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 328–692 Fragment：cytoplasmic fragment, residues 328-692 Mutation：T490M No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES NaOH pH 7.5, 27% (w/v) PEG 400, 0.23M NaCl Resolution 3.30 Å R-free 0.258
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 328–692 Fragment：cytoplasmic fragment, residues 328-692 Mutation：T490M No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES NaOH pH 7.5, 27% (w/v) PEG 400, 0.23M NaCl Resolution 3.30 Å R-free 0.258

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 6AI3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3A5I Structure of the cytoplasmic domain of FlhA Deposited 2009-08-07 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 328–692（365 aa） Fragment：FlhAc, UNP residues 328-692
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；10-15% PEG300, 4-6% PEG8000, 0.1M Tris-HCl, 0.5mM EDTA, 10-15% glycerol, pH8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.290
3A5I Structure of the cytoplasmic domain of FlhA Deposited 2009-08-07 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 328–692（365 aa） Fragment：FlhAc, UNP residues 328-692
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；10-15% PEG300, 4-6% PEG8000, 0.1M Tris-HCl, 0.5mM EDTA, 10-15% glycerol, pH8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.290
6AI0 Structure of the 328-692 fragment of FlhA (orthorhombic form) Deposited 2018-08-21 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692
Not recorded MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M HEPES NaOH pH 7.5, 10% (w/v) PEG-8000, 0.4M Ca(OAc)2
Resolution 2.40 Å R-free 0.277
6AI0 Structure of the 328-692 fragment of FlhA (orthorhombic form) Deposited 2018-08-21 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692
Not recorded MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M HEPES NaOH pH 7.5, 10% (w/v) PEG-8000, 0.4M Ca(OAc)2
Resolution 2.40 Å R-free 0.277
6AI1 Structure of the 328-692 fragment of FlhA (D456V) Deposited 2018-08-21 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692
Mutation：D456V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG-400, 0.1M HEPES pH 7.5, 0.25M NaCl
Resolution 3.50 Å R-free 0.241
6AI1 Structure of the 328-692 fragment of FlhA (D456V) Deposited 2018-08-21 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692
Mutation：D456V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG-400, 0.1M HEPES pH 7.5, 0.25M NaCl
Resolution 3.50 Å R-free 0.241
6AI2 Structure of the 328-692 fragment of FlhA (F459A) Deposited 2018-08-21 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692
Mutation：F459A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.2；293 K；20% (w/v) PEG 3350, 0.15M K2HPO4
Resolution 3.30 Å R-free 0.257
6AI2 Structure of the 328-692 fragment of FlhA (F459A) Deposited 2018-08-21 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692
Mutation：F459A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.2；293 K；20% (w/v) PEG 3350, 0.15M K2HPO4
Resolution 3.30 Å R-free 0.257
6CH1 Crystal structure of the cytoplasmic domain of FlhA in monomeric form Deposited 2018-02-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 360–692（333 aa） Fragment：UNP residues 360-692
Not recorded EDO 1,2-ETHANEDIOL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；tri-ammonium citrate, PEG3350
Resolution 1.90 Å R-free 0.237
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 conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 360–692（333 aa） Fragment：unp residues 360-692
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 conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 360–692（333 aa） Fragment：unp residues 360-692
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 conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 360–692（333 aa） Fragment：unp residues 360-692
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
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 conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 360–690（331 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
7CTN Structure of the 328-692 fragment of FlhA (E351A/D356A) Deposited 2020-08-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 328–692（365 aa）
Mutation：E351A/D356A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1M Tirs HCl pH 8.5, 20 % (w/v) PEG 8000, 0.2M MgCl2
Resolution 2.80 Å R-free 0.290
7CTN Structure of the 328-692 fragment of FlhA (E351A/D356A) Deposited 2020-08-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 328–692（365 aa）
Mutation：E351A/D356A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1M Tirs HCl pH 8.5, 20 % (w/v) PEG 8000, 0.2M MgCl2
Resolution 2.80 Å R-free 0.290

8 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLHA_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 5–369； UniProt 328–692 Author chain B； PDBConstruct 5–369； UniProt 328–692

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 6ai3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ai3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ai3
Deposition date deposition_date2018-08-21
Structure title titleStructure of the 328-692 fragment of FlhA (T490M)
Keywords keywordsflagellar type III secretion, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier31.31 Å
Radius of gyration Rg (electron density) rg_electron30.50 Å
Forward intensity I(0) i091490700.00
Molecular weight molecular_weight76014.0 kDa
Excluded volume excluded_volume95753 ų
Envelope volume envelope_volume132230 ų
Hydration-shell volume shell_volume36894 ų
Envelope diameter envelope_diameter109.7 Å
Shell Rg shell_rg36.86 Å
Envelope Rg envelope_rg30.36 Å
Shape Rg shape_rg30.51 Å
Total Rg total_rg31.11 Å
Total atoms total_atoms5348
Residues n_residues690
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 dmax104.9 Å
Rg (real space) rg_real31.27 Å
Rg uncertainty (real space) rg_real_error0.91 Å
I(0) (real space) i0_real9.1490e+07
I(0) uncertainty (real space) i0_real_error1.4940e+06
Rg (reciprocal space) rg_reciprocal31.29 Å
I(0) (reciprocal space) i0_reciprocal91490000.0000
Solution quality estimate total_estimate0.8799
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1 Å
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.225
Angular range angular_range— – 0.2550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17660000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.968
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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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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6ai3A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily60 — FHIPEP family, domain 1
Domain ID domain_id6ai3B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily60 — FHIPEP family, domain 1
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8. Citations (1)

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9. Files and Curves (10)