SAXSdb — 6ai0

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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)

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	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
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	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

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 6AI0	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 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：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 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：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
6AI1 Structure of the 328-692 fragment of FlhA (D456V) 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	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 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	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 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	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 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	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
6AI3 Structure of the 328-692 fragment of FlhA (T490M) 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	Mutation：T490M	No recorded non-water small molecule	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
6AI3 Structure of the 328-692 fragment of FlhA (T490M) 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	Mutation：T490M	No recorded non-water small molecule	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
6CH1 Crystal structure of the cytoplasmic domain of FlhA in monomeric form Deposited 2018-02-21	Different construct 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 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 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 360–690（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 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）	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 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）	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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6ai0
Deposition date deposition_date	2018-08-21
Structure title title	Structure of the 328-692 fragment of FlhA (orthorhombic form)
Keywords keywords	flagellar type III secretion, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	33.11 Å
Radius of gyration Rg (electron density) rg_electron	32.78 Å
Forward intensity I(0) i0	84031500.00
Molecular weight molecular_weight	73821.0 kDa
Excluded volume excluded_volume	93149 Å³
Envelope volume envelope_volume	125270 Å³
Hydration-shell volume shell_volume	33605 Å³
Envelope diameter envelope_diameter	116.8 Å
Shell Rg shell_rg	37.44 Å
Envelope Rg envelope_rg	32.65 Å
Shape Rg shape_rg	32.76 Å
Total Rg total_rg	33.24 Å
Total atoms total_atoms	5189
Residues n_residues	668
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	114.1 Å
Rg (real space) rg_real	33.27 Å
Rg uncertainty (real space) rg_real_error	0.85 Å
I(0) (real space) i0_real	8.4030e+07
I(0) uncertainty (real space) i0_real_error	1.3770e+06
Rg (reciprocal space) rg_reciprocal	33.21 Å
I(0) (reciprocal space) i0_reciprocal	84030000.0000
Solution quality estimate total_estimate	0.6482
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	40.4 Å
Skewness Skewness skewness	0.443
Kurtosis Kurtosis kurtosis	-0.198
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12750000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 0.049; Positv: 1.000; Valcen: 0.920; Smooth: 0.876

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Flagellar biosynthesis protein FlhA
Molecular weight formula_weight	40671.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5357

GPLGRGREEKAPEEPQPVKMPENNSVVEATWNDVQLEDSLGMEVGYRLIPMVDFQQDGELLGRIRSIRKKFAQDMGFLPPVVHIRDNMDLQPARYRILMKGVEIGSGDAYPGRWLAINPGTAAGTLPGEKTVDPAFGLDAIWIESALKEQAQIQGFTVVEASTVVATHLNHLIGQFSAELFGRQEAQQLLDRVSQEMPKLTEDLVPGVVTLTTLHKVLQNLLAEKVPIRDMRTILETLAEHAPLQSDPHELTAVVRVALGRAITQQWFPGNEEVQVIGLDTALERLLLQALQGGGGLEPGLADRLLAQTQEALSRQEMLGAPPVLLVNHALRPLLSRFLRRSLPQLVVLSNLELSDNRHIRMTATIGGK

来源 Source

来源生物 organism	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
NCBI Class编号 ncbi_taxonomy_id	99287
宿主生物 host_organism	Salmonella enterica subsp. enterica serovar Typhimurium

Entity 2 Entity 2 non-polymer

Description description	(4R)-2-METHYLPENTANE-2,4-DIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	168

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	6ai0A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	60 — FHIPEP family, domain 1

Domain ID domain_id	6ai0B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	60 — FHIPEP family, domain 1

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8. Citations (1)

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Unit-cell length a length_a	52.920 Å
Unit-cell length b length_b	93.080 Å
Unit-cell length c length_c	187.060 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	41.281 Å
R factor r_factor	0.2424
R_work r_work	0.2406
R_free r_free	0.2769

fit	/app/data/saxs_computation/ai/6ai0/6ai0.fit
pddf	/app/data/pr_computation/ai/6ai0/6ai0.pr.out
profile	/app/data/saxs_computation/ai/6ai0/6ai0.dat

Structure of the 328-692 fragment of FlhA (orthorhombic form)

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

Flagellar biosynthesis protein FlhA

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

Refinement Refinement

Diffraction experiment Diffraction