9txo

Spinach Ferredoxin I, Re-Oxidised

Method: X-RAY DIFFRACTION Dmax: 48.6 Å Quality: GOOD

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

Ferredoxin-1, chloroplastic

Spinacia oleracea

UniProt P00221

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 51–147 Not recorded FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;277 K;3.5M Ammonium Sulfate, 0.1M Sodium phosphate pH 7.8, 5% Glycerol Resolution 1.20 Å R-free 0.216

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FER1_SPIOL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–105; UniProt 51–147

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 9txo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9txo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9txo
Deposition date deposition_date2026-01-16
最后修订 last_revision2026-05-13
Structure title titleSpinach Ferredoxin I, Re-Oxidised
Keywords keywordsRedox, metalloprotein, iron-sulfur cluster, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.96
Radius of gyration Rg (electron density) rg_electron12.58
Forward intensity I(0) i02813890.00
Molecular weight molecular_weight10971.0 kDa
Excluded volume excluded_volume13346 ų
Envelope volume envelope_volume14998 ų
Hydration-shell volume shell_volume10267 ų
Envelope diameter envelope_diameter47.0
Shell Rg shell_rg18.23
Envelope Rg envelope_rg13.18
Shape Rg shape_rg12.63
Total Rg total_rg13.70
Total atoms total_atoms761
Residues n_residues100
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax48.6
Rg (real space) rg_real13.89
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real2.8140e+06
I(0) uncertainty (real space) i0_real_error3.2490e+04
Rg (reciprocal space) rg_reciprocal13.90
I(0) (reciprocal space) i0_reciprocal2814000.0000
Solution quality estimate total_estimate0.8480
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.122
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha419200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.680; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)