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10jx

Crystal structure of heme binding PAS domain from one component transcription factor, FG214

Method: X-RAY DIFFRACTION Dmax: 87.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Multi-sensor signal transduction histidine kinase

Fimbriimonas ginsengisoli Gsoil 348

UniProt A0A068NTE8

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 78–219 Chain B； UniProt 78–219 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 2 IMD IMIDAZOLE × 2 PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 1 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 3 MG MAGNESIUM ION × 1 FMT FORMIC ACID × 1 POL N-PROPANOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；298 K；0.2M Sodium formate, 0.2M Ammonium acetate, 0.2M Sodium citrate tribasic dihydrate, 0.2M Potassium sodium tartrate tetrahydrate, 0.2M Sodium oxamate, 0.2M 1,6-Hexanediol, 0.2M 1-Butanol 0.2M 1,2-Propanediol, 0.2M 2-Propanol, 0.2M 1,4-Butanediol, 0.2M 1,3-Propanediol, 0.4M Imidazole, 0.6M MES monohydrate, 25% v/v MPD, 25% PEG 1000, 25% w/v PEG 3350 Resolution 1.47 Å R-free 0.190

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 10JX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
10JY Crystal structure of heme binding PAS domain from one component transcription factor, FG214 reduced with dithionite Deposited 2026-01-22 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 78–219（142 aa）
Chain B 78–219（142 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 2 FMT FORMIC ACID × 2 PO4 PHOSPHATE ION × 1 POL N-PROPANOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.2M Sodium formate, 0.2M Ammonium acetate, 0.2M Sodium citrate tribasic dihydrate, 0.2M Potassium sodium tartrate tetrahydrate, 0.2M Sodium oxamate, 0.2M 1,6-Hexanediol, 0.2M 1-Butanol 0.2M 1,2-Propanediol, 0.2M 2-Propanol, 0.2M 1,4-Butanediol, 0.2M 1,3-Propanediol, 0.4M Imidazole, 0.6M MES monohydrate, 25% v/v MPD, 25% PEG 1000, 25% w/v PEG 3350
Resolution 1.65 Å R-free 0.215

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A068NTE8_FIMGI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 4–145； UniProt 78–219 Author chain B； PDBConstruct 4–145； UniProt 78–219

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 10jx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10jx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10jx
Deposition date deposition_date2026-01-22
最后修订 last_revision2026-03-25
Structure title titleCrystal structure of heme binding PAS domain from one component transcription factor, FG214
Keywords keywordstranscription factor, heme, PAS domain, bacterial signaling, TRANSCRIPTION; TRANSCRIPTION
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_guinier24.57 Å
Radius of gyration Rg (electron density) rg_electron24.59 Å
Forward intensity I(0) i019827200.00
Molecular weight molecular_weight33522.0 kDa
Excluded volume excluded_volume41803 ų
Envelope volume envelope_volume52541 ų
Hydration-shell volume shell_volume20022 ų
Envelope diameter envelope_diameter90.9 Å
Shell Rg shell_rg28.09 Å
Envelope Rg envelope_rg25.48 Å
Shape Rg shape_rg24.55 Å
Total Rg total_rg25.13 Å
Total atoms total_atoms2355
Residues n_residues282
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 dmax87.3 Å
Rg (real space) rg_real24.88 Å
Rg uncertainty (real space) rg_real_error0.77 Å
I(0) (real space) i0_real1.9830e+07
I(0) uncertainty (real space) i0_real_error2.8630e+05
Rg (reciprocal space) rg_reciprocal24.81 Å
I(0) (reciprocal space) i0_reciprocal19830000.0000
Solution quality estimate total_estimate0.8074
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6 Å
Skewness Skewness skewness0.633
Kurtosis Kurtosis kurtosis-0.076
Angular range angular_range— – 0.3250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3480000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.641; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.601; Smooth: 0.968
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (11)

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8. Citations (1)

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9. Files and Curves (10)