SAXSdb — 3fjo

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

NADPH-cytochrome P450 reductase

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 232–677	Fragment：yeast FMN domain, UNP residues 44-211, human FAD domain CPR, UNP residues 232-677	FMN FLAVIN MONONUCLEOTIDE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEGII from Nextal condition G11, pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.290

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 3FJO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B1C CRYSTAL STRUCTURE OF THE FMN-BINDING DOMAIN OF HUMAN CYTOCHROME P450 REDUCTASE AT 1.93A RESOLUTION Deposited 1998-11-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 61–241（181 aa） Fragment：FMN-BINDING DOMAIN	Not recorded	CA CALCIUM ION × 1 FMN FLAVIN MONONUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；18-20% (W/V) PEG400, 100 MM HEPES (PH6.8-7.2), 200 MM CACL2 4 DEGREES C, pH 7.0	Resolution 1.93 Å R-free 0.243
3QE2 Crystal Structure of Human NADPH-Cytochrome P450 Reductase Deposited 2011-01-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 64–677（614 aa） Fragment：UNP residues 64-677	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100 mM MES, 50 mM calcium acetate, 0.5 M sodium chloride, 14% PEG4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292KK	Resolution 1.75 Å R-free 0.239
3QE2 Crystal Structure of Human NADPH-Cytochrome P450 Reductase Deposited 2011-01-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 64–677（614 aa） Fragment：UNP residues 64-677	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100 mM MES, 50 mM calcium acetate, 0.5 M sodium chloride, 14% PEG4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292KK	Resolution 1.75 Å R-free 0.239
3QFC Crystal Structure of Human NADPH-Cytochrome P450 (V492E mutant) Deposited 2011-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 64–677（614 aa） Fragment：UNP residues 64-677	Mutation：V489E	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100 mM MES, 50 mM calcium acetate, 0.5 M sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292KK	Resolution 1.80 Å R-free 0.265
3QFC Crystal Structure of Human NADPH-Cytochrome P450 (V492E mutant) Deposited 2011-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 64–677（614 aa） Fragment：UNP residues 64-677	Mutation：V489E	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100 mM MES, 50 mM calcium acetate, 0.5 M sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292KK	Resolution 1.80 Å R-free 0.265
3QFR Crystal Structure of Human NADPH-Cytochrome P450 Reductase (R457H Mutant) Deposited 2011-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 64–677（614 aa） Fragment：UNP residues 64-677	Mutation：R454H	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100 mM MES, 50 mM calcium acetate, 0.1 M sodium chloride, 14% PEG4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.40 Å R-free 0.285
3QFR Crystal Structure of Human NADPH-Cytochrome P450 Reductase (R457H Mutant) Deposited 2011-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 64–677（614 aa） Fragment：UNP residues 64-677	Mutation：R454H	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100 mM MES, 50 mM calcium acetate, 0.1 M sodium chloride, 14% PEG4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.40 Å R-free 0.285
3QFS Crystal Structure of NADPH-Cytochrome P450 Reductase (FAD/NADPH domain) Deposited 2011-01-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 241–677（437 aa） Fragment：FAD/NADPH domain (UNP residues 241-677)	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；292 K；100 mM magnesium chloride, 15% PEG5000 MME, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.40 Å R-free 0.231
3QFT Crystal Structure of NADPH-Cytochrome P450 Reductase (FAD/NADPH domain and R457H Mutant) Deposited 2011-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 241–677（437 aa） Fragment：FAD/NADPH domain (UNP residues 241-677)	Mutation：R454H	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；292 K；100 mM magnesium chloride, 15% PEG5000 MME, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.40 Å R-free 0.227
5EMN Crystal Structure of Human NADPH-Cytochrome P450 Reductase(A287P mutant) Deposited 2015-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 64–677（614 aa） Fragment：UNP residues 57-677	Mutation：P228L, A287P, A503V	FMN FLAVIN MONONUCLEOTIDE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100mM MES,pH6.5,50mM CaAc2,0.1M NaCl, 14% PEG4K	Resolution 2.20 Å R-free 0.277
5EMN Crystal Structure of Human NADPH-Cytochrome P450 Reductase(A287P mutant) Deposited 2015-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 64–677（614 aa） Fragment：UNP residues 57-677	Mutation：P228L, A287P, A503V	FMN FLAVIN MONONUCLEOTIDE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；100mM MES,pH6.5,50mM CaAc2,0.1M NaCl, 14% PEG4K	Resolution 2.20 Å R-free 0.277
5FA6 wild type human CYPOR Deposited 2015-12-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 64–677（614 aa） Fragment：UNP residues 64-677	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；MES buffer, PEG 4K, CaAc2 and NaCl	Resolution 2.30 Å R-free 0.280
5FA6 wild type human CYPOR Deposited 2015-12-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 64–677（614 aa） Fragment：UNP residues 64-677	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；292 K；MES buffer, PEG 4K, CaAc2 and NaCl	Resolution 2.30 Å R-free 0.280

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

View Construct and Data Evidence

UniProt name	NCPR_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 192–637； UniProt 232–677

NADPH-cytochrome P450 reductase

Homo sapiens

UniProt P16603

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 44–211	Fragment：yeast FMN domain, UNP residues 44-211, human FAD domain CPR, UNP residues 232-677	FMN FLAVIN MONONUCLEOTIDE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEGII from Nextal condition G11, pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.290

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 3FJO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BF4 A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases. Deposited 2004-12-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 46–690（645 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；293 K；1.6 M AMMONIUM SULFATE,100 MM SODIUM CITRATE (PH 5.0),T=20 C	Resolution 3.00 Å R-free 0.261
2BF4 A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases. Deposited 2004-12-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 46–690（645 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；293 K；1.6 M AMMONIUM SULFATE,100 MM SODIUM CITRATE (PH 5.0),T=20 C	Resolution 3.00 Å R-free 0.261
2BN4 A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductase Deposited 2005-03-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 46–690（645 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；293 K；1.6 M AMMONIUM SULFATE 100 MM SODIUM CITRATE (PH 5.0) 1 MM FAD 1 MM NADPH T=20 C	Resolution 2.91 Å R-free 0.300
2BN4 A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductase Deposited 2005-03-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 47–690（644 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；293 K；1.6 M AMMONIUM SULFATE 100 MM SODIUM CITRATE (PH 5.0) 1 MM FAD 1 MM NADPH T=20 C	Resolution 2.91 Å R-free 0.300
2BPO Crystal structure of the yeast CPR triple mutant: D74G, Y75F, K78A. Deposited 2005-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 46–690（645 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；295 K；1.6 M AMMONIUM SULFATE 100 MM SODIUM CITRATE, PH 5.0 5 MM NICKEL CHLORIDE 1 MM FMN 1 MM FAD 1 MM NADP, T=22 C.	Resolution 2.90 Å R-free 0.268
2BPO Crystal structure of the yeast CPR triple mutant: D74G, Y75F, K78A. Deposited 2005-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 46–690（645 aa）	Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；295 K；1.6 M AMMONIUM SULFATE 100 MM SODIUM CITRATE, PH 5.0 5 MM NICKEL CHLORIDE 1 MM FMN 1 MM FAD 1 MM NADP, T=22 C.	Resolution 2.90 Å R-free 0.268

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

View Construct and Data Evidence

UniProt name	NCPR_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 24–191； UniProt 44–211

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3fjo
Deposition date deposition_date	2008-12-15
Structure title title	Structure of chimeric YH CPR
Keywords keywords	;FMN and FAD domains of CPR, OXIDOREDUCTASE, Endoplasmic reticulum, Flavoprotein, Membrane, NADP, Phosphoprotein, Transmembrane, Congenital adrenal hyperplasia, Disease mutation ;; 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	36.31 Å
Radius of gyration Rg (electron density) rg_electron	36.19 Å
Forward intensity I(0) i0	76576500.00
Molecular weight molecular_weight	68925.0 kDa
Excluded volume excluded_volume	85787 Å³
Envelope volume envelope_volume	116320 Å³
Hydration-shell volume shell_volume	29313 Å³
Envelope diameter envelope_diameter	122.3 Å
Shell Rg shell_rg	39.04 Å
Envelope Rg envelope_rg	35.16 Å
Shape Rg shape_rg	36.23 Å
Total Rg total_rg	36.26 Å
Total atoms total_atoms	4853
Residues n_residues	603
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	120.6 Å
Rg (real space) rg_real	36.68 Å
Rg uncertainty (real space) rg_real_error	1.03 Å
I(0) (real space) i0_real	7.6580e+07
I(0) uncertainty (real space) i0_real_error	1.3910e+06
Rg (reciprocal space) rg_reciprocal	36.46 Å
I(0) (reciprocal space) i0_reciprocal	76560000.0000
Solution quality estimate total_estimate	0.7892
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	27.4 Å
Skewness Skewness skewness	0.424
Kurtosis Kurtosis kurtosis	-0.730
Angular range angular_range	— – 0.2200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12670000.0000
Real-space data points n_real_points	45
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.695; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.487; Smooth: 0.682

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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	NADPH-cytochrome P450 reductase
Molecular weight formula_weight	71419.3 kDa
EC 编号 ec_number	1.6.2.4
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	4976

MGSSHHHHHHSSGLVPRGSHMLESSGNRDIAQVVTENNKNYLVLYASQTGTAEDYAKKFSKELVAKFNLNVMCADVENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLRYNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDYMAWKDSILEVLKDELGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPFIGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQSHKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVDYIKKLMTKGRYSLDVWS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	;Baker's yeast, Human ;
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	FLAVIN MONONUCLEOTIDE
Molecular weight formula_weight	456.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 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 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	123

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d3fjoa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.5 — Flavoproteins
Family Family family	c.23.5.0 — automated matches

Domain ID domain_id	d3fjoa2
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.43.4.1 — NADPH-cytochrome p450 reductase FAD-binding domain-like

Domain ID domain_id	d3fjoa3
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.25.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	3fjoA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	360 — Flavodoxin domain

Domain ID domain_id	3fjoA03
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	3fjoA04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	990 — NADPH-cytochrome p450 Reductase; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — NADPH-cytochrome p450 Reductase; Chain A, domain 3

Domain ID domain_id	3fjoA05
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 (1)

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Unit-cell length a length_a	146.800 Å
Unit-cell length b length_b	60.700 Å
Unit-cell length c length_c	78.860 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.36 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	19.860 Å
R factor r_factor	0.2255
R_work r_work	0.2221
R_free r_free	0.2899

fit	/app/data/saxs_computation/fj/3fjo/3fjo.fit
pddf	/app/data/pr_computation/fj/3fjo/3fjo.pr.out
profile	/app/data/saxs_computation/fj/3fjo/3fjo.dat

Structure of chimeric YH CPR

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

NADPH-cytochrome P450 reductase

State in the Current Structure

Other States of the Same Protein in the Database

NADPH-cytochrome P450 reductase

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)