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1fnc

REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES

Method: X-RAY DIFFRACTION Dmax: 64.0 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

FERREDOXIN-NADP+ REDUCTASE

Spinacia oleracea

UniProt P00455

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 56–369 Not recorded SO4 SULFATE ION × 1 FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE × 1 A2P ADENOSINE-2'-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å

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 1FNC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BX0 Ferredoxin:nadp+ oxidoreductase (ferredoxin reductase) mutant e312l Deposited 1998-10-10 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 56–369（314 aa）
Mutation：E312L PO4 PHOSPHATE ION × 1 SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 1.90 Å
1BX1 FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312Q Deposited 1998-10-10 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 56–369（314 aa）
Mutation：E312Q PO4 PHOSPHATE ION × 1 SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 1.90 Å
1FNB REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES Deposited 1995-01-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 56–369（314 aa）
Not recorded PO4 PHOSPHATE ION × 1 SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PH 4.6
Resolution 1.70 Å
1FND REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES Deposited 1995-01-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 56–369（314 aa）
Not recorded SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 A2P ADENOSINE-2'-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PH 4.6
Resolution 1.70 Å
1FRN THE INVOLVEMENT OF SER96 IN THE CATALYTIC MECHANISM OF FERREDOXIN-NADP+ REDUCTASE: STRUCTURE-FUNCTION RELATIONSHIP AS STUDIED BY SITE-DIRECTED MUTAGENESIS AND X-RAY CRYSTALLOGRAPHY Deposited 1995-03-31 Different ligand/ion Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 56–369（314 aa）
Not recorded PO4 PHOSPHATE ION × 1 SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1FRQ FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312A Deposited 1998-10-10 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 56–369（314 aa）
Mutation：E312A PO4 PHOSPHATE ION × 1 SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 1.95 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FENR_SPIOL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–314； UniProt 56–369

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 1fnc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fnc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1fnc
Deposition date deposition_date1995-01-05
Structure title titleREFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES
Keywords keywordsOXIDOREDUCTASE (NADP+(A), FERREDOXIN(A)); OXIDOREDUCTASE (NADP+(A),FERREDOXIN(A))
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_guinier20.62 Å
Radius of gyration Rg (electron density) rg_electron19.48 Å
Forward intensity I(0) i021250800.00
Molecular weight molecular_weight34815.0 kDa
Excluded volume excluded_volume43403 ų
Envelope volume envelope_volume50275 ų
Hydration-shell volume shell_volume21284 ų
Envelope diameter envelope_diameter63.7 Å
Shell Rg shell_rg26.31 Å
Envelope Rg envelope_rg19.85 Å
Shape Rg shape_rg19.49 Å
Total Rg total_rg20.34 Å
Total atoms total_atoms2437
Residues n_residues296
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 dmax64.0 Å
Rg (real space) rg_real20.52 Å
Rg uncertainty (real space) rg_real_error0.36 Å
I(0) (real space) i0_real2.1250e+07
I(0) uncertainty (real space) i0_real_error2.8110e+05
Rg (reciprocal space) rg_reciprocal20.54 Å
I(0) (reciprocal space) i0_reciprocal21250000.0000
Solution quality estimate total_estimate0.9047
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1 Å
Skewness Skewness skewness0.189
Kurtosis Kurtosis kurtosis-0.432
Angular range angular_range— – 0.3850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3430000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.996
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fnca1
Class classb — All beta proteins
Fold Fold foldb.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamilyb.43.4 — Riboflavin synthase domain-like
Family Family familyb.43.4.2 — Ferredoxin reductase FAD-binding domain-like
Domain ID domain_idd1fnca2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.25 — Ferredoxin reductase-like, C-terminal NADP-linked domain
Superfamily Superfamily superfamilyc.25.1 — Ferredoxin reductase-like, C-terminal NADP-linked domain
Family Family familyc.25.1.1 — Reductases

CATH v4.4 (2 domains)

Domain ID domain_id1fncA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id1fncA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily80 — Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
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8. Citations (2)

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9. Files and Curves (10)