SAXSdb — 6ch1

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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 360–692	Fragment：UNP residues 360-692	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

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 6CH1	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
6AI0 Structure of the 328-692 fragment of FlhA (orthorhombic form) Deposited 2018-08-21	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 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 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：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 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） 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 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） 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 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） 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 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） 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 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） 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 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） 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
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 16 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 5–337； UniProt 360–692

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	6ch1
Deposition date deposition_date	2018-02-21
Structure title title	Crystal structure of the cytoplasmic domain of FlhA in monomeric form
Keywords keywords	flagellar, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
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	23.70 Å
Radius of gyration Rg (electron density) rg_electron	22.59 Å
Forward intensity I(0) i0	23110200.00
Molecular weight molecular_weight	37049.0 kDa
Excluded volume excluded_volume	46710 Å³
Envelope volume envelope_volume	57785 Å³
Hydration-shell volume shell_volume	21665 Å³
Envelope diameter envelope_diameter	73.6 Å
Shell Rg shell_rg	28.95 Å
Envelope Rg envelope_rg	22.58 Å
Shape Rg shape_rg	22.60 Å
Total Rg total_rg	23.42 Å
Total atoms total_atoms	5280
Residues n_residues	332
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	72.8 Å
Rg (real space) rg_real	23.61 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	2.3110e+07
I(0) uncertainty (real space) i0_real_error	3.1540e+05
Rg (reciprocal space) rg_reciprocal	23.64 Å
I(0) (reciprocal space) i0_reciprocal	23110000.0000
Solution quality estimate total_estimate	0.9133
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.6 Å
Skewness Skewness skewness	0.160
Kurtosis Kurtosis kurtosis	-0.597
Angular range angular_range	— – 0.3350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4676000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.977

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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 biosynthesis protein FlhA
Molecular weight formula_weight	36982.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5519

QGGGEDSLGMEVGYRLIPMVDFQQDGELLGRIRSIRKKFAQDMGFLPPVVHIRDNMDLQPARYRILMKGVEIGSGDAYPGRWLAINPGTAAGTLPGEKTVDPAFGLDAIWIESALKEQAQIQGFTVVEASTVVATHLNHLIGQFSAELFGRQEAQQLLDRVSQEMPKLTEDLVPGVVTLTTLHKVLQNLLAEKVPIRDMRTILETLAEHAPLQSDPHELTAVVRVALGRAITQQWFPGNEEVQVIGLDTALERLLLQALQGGGGLEPGLADRLLAQTQEALSRQEMLGAPPVLLVNHALRPLLSRFLRRSLPQLVVLSNLELSDNRHIRMTATIGGK

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	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	211

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	6ch1A01
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	40.380 Å
Unit-cell length b length_b	49.970 Å
Unit-cell length c length_c	50.950 Å
Unit-cell angle α angle_alpha	78.04 °
Unit-cell angle β angle_beta	68.99 °
Unit-cell angle γ angle_gamma	80.66 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	19.920 Å
R factor r_factor	0.2000
R_work r_work	0.1980
R_free r_free	0.2370

fit	/app/data/saxs_computation/ch/6ch1/6ch1.fit
pddf	/app/data/pr_computation/ch/6ch1/6ch1.pr.out
profile	/app/data/saxs_computation/ch/6ch1/6ch1.dat

Crystal structure of the cytoplasmic domain of FlhA in monomeric 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