1e62

Ferredoxin:NADP+ reductase mutant with Lys 75 replaced by Arg (K75R)

Method: X-RAY DIFFRACTION D_max: 63.3 Å Quality: GOOD

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

FERREDOXIN-NADP+ REDUCTASE

NOSTOC SP. PCC 7119

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 137–440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.5；pH 5.50	Resolution 2.30 Å R-free 0.250

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 1E62	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B2R FERREDOXIN-NADP+ REDUCTASE (MUTATION: E 301 A) Deposited 1998-11-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa）	Mutation：E301A	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.0	Resolution 1.80 Å R-free 0.240
1BJK FERREDOXIN:NADP+ REDUCTASE MUTANT WITH ARG 264 REPLACED BY GLU (R264E) Deposited 1998-06-25	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–440（295 aa）	Mutation：R264E	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.0	Resolution 2.30 Å R-free 0.224
1BQE FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY (T155G) Deposited 1998-08-14	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–440（295 aa）	Mutation：T155G	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.0	Resolution 2.45 Å R-free 0.240
1E63 Ferredoxin:NADP+ Reductase Mutant with LYS 75 Replaced by SER (K75S) Deposited 2000-08-07	Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.50	Resolution 2.30 Å R-free 0.240
1E64 FERREDOXIN:NADP+ REDUCTASE MUTANT WITH LYS 75 REPLACED BY GLN (K75Q) Deposited 2000-08-07	Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.50	Resolution 2.30 Å R-free 0.230
1EWY ANABAENA PCC7119 FERREDOXIN:FERREDOXIN-NADP+-REDUCTASE COMPLEX Deposited 2000-04-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 138–440（303 aa） Fragment：138-440	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；20-24% PEG 6000,10 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.38 Å R-free 0.293
1EWY ANABAENA PCC7119 FERREDOXIN:FERREDOXIN-NADP+-REDUCTASE COMPLEX Deposited 2000-04-28	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 138–440（303 aa） Fragment：138-440	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；20-24% PEG 6000,10 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.38 Å R-free 0.293
1GJR Ferredoxin-NADP+ Reductase complexed with NADP+ by COCRYSTALLIZATION Deposited 2001-08-01	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 137–440（304 aa） Fragment：RESIDUES 137-440	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 2.10 Å R-free 0.270
1GO2 Structure of Ferredoxin-NADP+ Reductase with Lys 72 replaced by Glu (K72E) Deposited 2001-10-15	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 1.70 Å R-free 0.250
1GR1 Structure of Ferredoxin-NADP+ Reductase with Glu 139 replaced by Lys (E139K) Deposited 2001-12-12	Different construct Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.50	Resolution 2.50 Å R-free 0.250
1H42 FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR AND LEU 263 REPLACED BY PRO (T155G-A160T-L263P) Deposited 2002-09-26	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 2.15 Å R-free 0.231
1H85 FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L) Deposited 2001-01-24	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–440（295 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 2.30 Å R-free 0.260
1OGI FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY AND ALA 160 REPLACED BY THR (T155G-A160T) Deposited 2003-05-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa） Fragment：RESIDUES 138-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 1.64 Å R-free 0.221
1OGJ FERREDOXIN:NADP+ REDUCTASE MUTANT WITH LEU 263 REPLACED BY PRO (L263P) Deposited 2003-05-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa） Fragment：RESDIUES 138-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 1.64 Å R-free 0.228
1QGY Ferredoxin:NADP+ reductase mutant with Lys 75 replaced by Glu (K75E) Deposited 1999-05-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–440（295 aa）	Mutation：K75E	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.0	Resolution 1.70 Å R-free 0.230
1QGZ FERREDOXIN:NADP+ REDUCTASE MUTANT WITH LEU 78 REPLACED BY ASP (L78D) Deposited 1999-05-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–440（295 aa）	Mutation：L78D	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.0	Resolution 2.30 Å R-free 0.226
1QH0 FERREDOXIN:NADP+ REDUCTASE MUTANT WITH LEU 76 MUTATED BY ASP AND LEU 78 MUTATED BY ASP Deposited 1999-05-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–440（295 aa）	Mutation：L76D, L78D	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.0	Resolution 1.93 Å R-free 0.250
1QUE X-RAY STRUCTURE OF THE FERREDOXIN:NADP+ REDUCTASE FROM THE CYANOBACTERIUM ANABAENA PCC 7119 AT 1.8 ANGSTROMS Deposited 1996-07-06	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa）	Not recorded	SO4 SULFATE ION × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；SEE REFERENCE 1., pH 7.0, vapor diffusion - hanging drop	Resolution 1.80 Å R-free 0.214
1QUF X-RAY STRUCTURE OF A COMPLEX NADP+-FERREDOXIN:NADP+ REDUCTASE FROM THE CYANOBACTERIUM ANABAENA PCC 7119 AT 2.25 ANGSTROMS Deposited 1996-09-07	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 137–440（304 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；SEE REFERENCE 1., pH 5.5	Resolution 2.25 Å R-free 0.265
1W34 FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 S) Deposited 2004-07-13	Different construct Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.50	Resolution 1.73 Å R-free 0.208
1W35 FERREDOXIN-NADP+ REDUCTASE (MUTATION: Y 303 W) Deposited 2004-07-13	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 1.90 Å R-free 0.204
1W87 FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION Deposited 2004-09-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 3.00 Å R-free 0.272
1W87 FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION Deposited 2004-09-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 3.00 Å R-free 0.272
2BMW Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr, Leu 263 Replaced By Pro, Arg 264 Replaced By Pro and Gly 265 Replaced by Pro (T155G-A160T-L263P-R264P-G265P) Deposited 2005-03-16	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；pH 5.00	Resolution 1.50 Å R-free 0.207
2BSA Ferredoxin-Nadp Reductase (Mutation: Y 303 S) complexed with NADP Deposited 2005-05-20	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.50	Resolution 1.92 Å R-free 0.219
2VYQ FERREDOXIN:NADP REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO AND TYR 303 REPLACED BY SER (T155G-A160T-L263P-Y303S) Deposited 2008-07-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；18-20 % (W/V) PEG 6000 20 MM AMMONIUM SULPHATE 0.1M MES/NAOH, PH 5.0-5.5 B-OCTYL GLYCOSIDE AT 2%(W/V)	Resolution 1.90 Å R-free 0.185
2VZL FERREDOXIN-NADP REDUCTASE (MUTATIONS: T155G, A160T, L263P AND Y303S) COMPLEXED WITH NAD BY COCRYSTALLIZATION Deposited 2008-07-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–440（304 aa） Fragment：RESIDUES 137-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG 6000 0.1M ACNA, PH 5.5 B-OCTYL GLYCOSIDE AT 2%(W/V) 10-60 MM NAD	Resolution 1.93 Å R-free 0.195
2X3U Ferredoxin-NADP reductase mutant with Tyr 303 replaced by Phe (Y303F) Deposited 2010-01-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18 % PEG 6000, 0.1 M NAAC PH 5.5, 20 MM (NH4)2SO4	Resolution 1.93 Å R-free 0.205
3ZBT Ferredoxin-NADP Reductase Mutant with SER 59 Replaced by ALA (S59A) Deposited 2012-11-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa） Fragment：RESIDUES 138-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18 % PEG 6000, 0.1 M NAAC PH 5.5, 20 MM (NH4)2SO4	Resolution 1.92 Å R-free 0.238
3ZBU Ferredoxin-NADP Reductase Mutant with SER 80 Replaced by ALA (S80A) Deposited 2012-11-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa） Fragment：RESIDUES 138-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 GOL GLYCEROL × 4 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18 % PEG 6000, 0.1 M NAAC PH 5.5, 20 MM (NH4)2SO4	Resolution 1.89 Å R-free 0.205
3ZC3 FERREDOXIN-NADP REDUCTASE (MUTATION S80A) COMPLEXED WITH NADP BY COCRYSTALLIZATION Deposited 2012-11-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18% PEG 6000, 0.1 NAAC PH 5.5, 10 MM NADP	Resolution 2.30 Å R-free 0.246
3ZC3 FERREDOXIN-NADP REDUCTASE (MUTATION S80A) COMPLEXED WITH NADP BY COCRYSTALLIZATION Deposited 2012-11-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 138–440（303 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18% PEG 6000, 0.1 NAAC PH 5.5, 10 MM NADP	Resolution 2.30 Å R-free 0.246
4BPR FERREDOXIN-NADP REDUCTASE MUTANT WITH TYR 79 REPLACED BY PHE (Y79F) Deposited 2013-05-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa） Fragment：RESIDUES 138-440	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18% PEG 6000, 0.1 M NAAC PH 5.5, 20 MM (NH4)2 SO4	Resolution 2.00 Å R-free 0.212
4C43 FERREDOXIN NADP REDUCTASE MUTANT WITH GLU 103 REPLACED BY TYR, TYR 104 REPLACED BY PHE, SER 109 REPLACED BY PHE AND GLY 110 REPLACED BY PRO (E103Y-Y104F-S109F-G110P) Deposited 2013-08-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 138–440（303 aa） Fragment：RESIDUES 138-440	Mutation：YES	SO4 SULFATE ION × 1 GOL GLYCEROL × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions 18-20% PEG 6000,20 MM AMMONIUM SULFATE, 0.1 M MES/NAOH, PH 5.0.	Resolution 1.70 Å R-free 0.205

31 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FENR_ANASO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–304； UniProt 137–440

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1e62
Deposition date deposition_date	2000-08-07
Structure title title	Ferredoxin:NADP+ reductase mutant with Lys 75 replaced by Arg (K75R)
Keywords keywords	OXIDOREDUCTASE, FLAVOPROTEIN, NADP, FAD, FNR, NADP REDUCTASE; OXIDOREDUCTASE
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	20.60 Å
Radius of gyration Rg (electron density) rg_electron	19.43 Å
Forward intensity I(0) i0	20427200.00
Molecular weight molecular_weight	34066.0 kDa
Excluded volume excluded_volume	42473 Å³
Envelope volume envelope_volume	49898 Å³
Hydration-shell volume shell_volume	21211 Å³
Envelope diameter envelope_diameter	63.1 Å
Shell Rg shell_rg	26.10 Å
Envelope Rg envelope_rg	19.74 Å
Shape Rg shape_rg	19.44 Å
Total Rg total_rg	20.28 Å
Total atoms total_atoms	2398
Residues n_residues	295
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	63.3 Å
Rg (real space) rg_real	20.49 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	2.0430e+07
I(0) uncertainty (real space) i0_real_error	2.4900e+05
Rg (reciprocal space) rg_reciprocal	20.51 Å
I(0) (reciprocal space) i0_reciprocal	20430000.0000
Solution quality estimate total_estimate	0.7651
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.8 Å
Skewness Skewness skewness	0.162
Kurtosis Kurtosis kurtosis	-0.464
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3336000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 0.387; Positv: 1.000; Valcen: 0.989; Smooth: 0.997

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	FERREDOXIN-NADP+ REDUCTASE
Molecular weight formula_weight	34200.9 kDa
EC 编号 ec_number	1.18.1.2
Mutation mutation	YES
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	2550

MTQAKAKHADVPVNLYRPNAPFIGKVISNEPLVKEGGIGIVQHIKFDLTGGNLKYIEGQSIGIIPPGVDKNGKPERLRLYSIASTRHGDDVDDKTISLCVRQLEYKHPESGETVYGVCSTYLTHIEPGSEVKITGPVGKEMLLPDDPEANVIMLATGTGIAPMRTYLWRMFKDAERAANPEYQFKGFSWLVFGVPTTPNILYKEELEEIQQKYPDNFRLTYAISREQKNPQGGRMYIQDRVAEHADQLWQLIKNQKTHTYICGLRGMEEGIDAALSAAAAKEGVTWSDYQKDLKKAGRWHVETY

来源 Source

来源生物 organism	NOSTOC SP. PCC 7119
NCBI Class编号 ncbi_taxonomy_id	1168
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	152

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1e62a1
Class class	b — All beta proteins
Fold Fold fold	b.43 — Reductase/isomerase/elongation factor common domain
Superfamily Superfamily superfamily	b.43.4 — Riboflavin synthase domain-like
Family Family family	b.43.4.2 — Ferredoxin reductase FAD-binding domain-like

Domain ID domain_id	d1e62a2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.25 — Ferredoxin reductase-like, C-terminal NADP-linked domain
Superfamily Superfamily superfamily	c.25.1 — Ferredoxin reductase-like, C-terminal NADP-linked domain
Family Family family	c.25.1.1 — Reductases

CATH v4.4 (2 domains)

Domain ID domain_id	1e62A01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	10 — Translation factors

Domain ID domain_id	1e62A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	80 — Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module

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8. Citations (2)

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Unit-cell length a length_a	88.180 Å
Unit-cell length b length_b	88.180 Å
Unit-cell length c length_c	97.200 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 65
Space-group number int_tables_number	170
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2000
R_work r_work	0.2000
R_free r_free	0.2500

fit	/app/data/saxs_computation/e6/1e62/1e62.fit
pddf	/app/data/pr_computation/e6/1e62/1e62.pr.out
profile	/app/data/saxs_computation/e6/1e62/1e62.dat