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2d4y

Crystal structure of a 49K fragment of HAP1 (FlgK)

Method: X-RAY DIFFRACTION Dmax: 111.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Flagellar hook-associated protein 1

Salmonella typhimurium

UniProt P0A1J5

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 65–526 Fragment：FK49 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 5.5；289 K；14-15% PEG 8000, 20-25% isopropanol, 0.1M citrate, pH 5.5, VAPOR DIFFUSION, temperature 289K Resolution 2.10 Å R-free 0.255
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 65–526 Fragment：FK49 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 5.5；289 K；14-15% PEG 8000, 20-25% isopropanol, 0.1M citrate, pH 5.5, VAPOR DIFFUSION, temperature 289K Resolution 2.10 Å R-free 0.255

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 2D4Y Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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 method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 73 PDB declaration: 73-meric
Chain CA 1–553（553 aa）
Chain CB 1–553（553 aa）
Chain CC 1–553（553 aa）
Chain CD 1–553（553 aa）
Chain CE 1–553（553 aa）
Chain CF 1–553（553 aa）
Chain CG 1–553（553 aa）
Chain CH 1–553（553 aa）
Chain CI 1–553（553 aa）
Chain CJ 1–553（553 aa）
Chain CK 1–553（553 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 method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric
Chain CA 1–553（553 aa）
Chain CB 1–553（553 aa）
Chain CC 1–553（553 aa）
Chain CD 1–553（553 aa）
Chain CE 1–553（553 aa）
Chain CF 1–553（553 aa）
Chain CG 1–553（553 aa）
Chain CH 1–553（553 aa）
Chain CI 1–553（553 aa）
Chain CJ 1–553（553 aa）
Chain CK 1–553（553 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

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

View Construct and Data Evidence
UniProt name FLGK_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–463； UniProt 65–526 Author chain B； PDBConstruct 2–463； UniProt 65–526

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 2d4y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2d4y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2d4y
Deposition date deposition_date2005-10-25
Structure title titleCrystal structure of a 49K fragment of HAP1 (FlgK)
Keywords keywordsMulti-domain protein, alpha-helical bundle, complex all-beta folds, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
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_guinier33.64 Å
Radius of gyration Rg (electron density) rg_electron32.96 Å
Forward intensity I(0) i0143317000.00
Molecular weight molecular_weight91621.0 kDa
Excluded volume excluded_volume113270 ų
Envelope volume envelope_volume149860 ų
Hydration-shell volume shell_volume38980 ų
Envelope diameter envelope_diameter123.6 Å
Shell Rg shell_rg38.48 Å
Envelope Rg envelope_rg32.83 Å
Shape Rg shape_rg32.96 Å
Total Rg total_rg33.41 Å
Total atoms total_atoms6441
Residues n_residues854
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 dmax111.7 Å
Rg (real space) rg_real33.66 Å
Rg uncertainty (real space) rg_real_error0.85 Å
I(0) (real space) i0_real1.4330e+08
I(0) uncertainty (real space) i0_real_error2.2750e+06
Rg (reciprocal space) rg_reciprocal33.65 Å
I(0) (reciprocal space) i0_reciprocal143300000.0000
Solution quality estimate total_estimate0.8809
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.8 Å
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.241
Angular range angular_range— – 0.2350 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16100000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.877
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)