2cfy

Crystal structure of human thioredoxin reductase 1

Method: X-RAY DIFFRACTION D_max: 199.3 Å Quality: GOOD

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

THIOREDOXIN REDUCTASE 1

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	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–499 Chain B； UniProt 1–499	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；150 UL SITTING DROPS, 20% PEG3350, 0.1 M TRIS PH 7, ADDITIVE: NSDB-221	Resolution 2.70 Å R-free 0.248
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–499 Chain D； UniProt 1–499	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；150 UL SITTING DROPS, 20% PEG3350, 0.1 M TRIS PH 7, ADDITIVE: NSDB-221	Resolution 2.70 Å R-free 0.248
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 1–499 Chain F； UniProt 1–499	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；150 UL SITTING DROPS, 20% PEG3350, 0.1 M TRIS PH 7, ADDITIVE: NSDB-221	Resolution 2.70 Å R-free 0.248

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 2CFY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2J3N X-ray structure of human thioredoxin reductase 1 Deposited 2006-08-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–499（499 aa） Chain B 1–499（499 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.287
2J3N X-ray structure of human thioredoxin reductase 1 Deposited 2006-08-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–499（499 aa） Chain D 1–499（499 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.287
2J3N X-ray structure of human thioredoxin reductase 1 Deposited 2006-08-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–499（499 aa） Chain F 1–499（499 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.287
2ZZ0 Crystal structure of human thioredoxin reductase I (SeCys 498 Cys) Deposited 2009-02-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 150–649（500 aa） Fragment：residues (-13)-499 Chain B 150–649（500 aa） Fragment：residues (-13)-499	Mutation：SeCys498Cys Mutation：SeCys498Cys	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；5% PEG 3350, 0.005M magnesium Sulfate, 0.05M MES, pH 6.0, 20% 1,6 Hexanediol (0.001mL), VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.80 Å R-free 0.277
2ZZ0 Crystal structure of human thioredoxin reductase I (SeCys 498 Cys) Deposited 2009-02-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 150–649（500 aa） Fragment：residues (-13)-499 Chain D 150–649（500 aa） Fragment：residues (-13)-499	Mutation：SeCys498Cys Mutation：SeCys498Cys	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；5% PEG 3350, 0.005M magnesium Sulfate, 0.05M MES, pH 6.0, 20% 1,6 Hexanediol (0.001mL), VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.80 Å R-free 0.277
2ZZB Crystal structure of human thioredoxin reductase I and terpyridine platinum(II) Deposited 2009-02-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 150–649（500 aa） Fragment：residues (-13)-499 Chain B 150–649（500 aa） Fragment：residues (-13)-499	Mutation：SeCys498Cys Mutation：SeCys498Cys	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 SO4 SULFATE ION × 2 TPT 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；5% PEG 3350, 0.005M magnesium Sulfate, 0.05M MES, pH 6.0, additive: 20% 1,6 Hexanediol (0.001mL), VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.20 Å R-free 0.305
2ZZB Crystal structure of human thioredoxin reductase I and terpyridine platinum(II) Deposited 2009-02-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 150–649（500 aa） Fragment：residues (-13)-499 Chain D 150–649（500 aa） Fragment：residues (-13)-499	Mutation：SeCys498Cys Mutation：SeCys498Cys	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 SO4 SULFATE ION × 2 TPT 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；5% PEG 3350, 0.005M magnesium Sulfate, 0.05M MES, pH 6.0, additive: 20% 1,6 Hexanediol (0.001mL), VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.20 Å R-free 0.305
2ZZC Crystal structure of NADP(H):human thioredoxin reductase I Deposited 2009-02-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 150–649（500 aa） Fragment：residues (-13)-499 Chain B 150–649（500 aa） Fragment：residues (-13)-499	Mutation：SeCys498Cys Mutation：SeCys498Cys	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；5% PEG 3350, 0.005M Magnesium Sulfate, 0.05M MES, pH 6.0, additive: 20% 1,6 Hexanediol (0.001mL), VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.60 Å R-free 0.260
2ZZC Crystal structure of NADP(H):human thioredoxin reductase I Deposited 2009-02-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 150–649（500 aa） Fragment：residues (-13)-499 Chain D 150–649（500 aa） Fragment：residues (-13)-499	Mutation：SeCys498Cys Mutation：SeCys498Cys	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；5% PEG 3350, 0.005M Magnesium Sulfate, 0.05M MES, pH 6.0, additive: 20% 1,6 Hexanediol (0.001mL), VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.60 Å R-free 0.260
3QFA Crystal structure of the human thioredoxin reductase-thioredoxin complex Deposited 2011-01-21	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–499（499 aa） Chain B 1–499（499 aa）	Mutation：C497S, U498C Mutation：C497S, U498C	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；297.15 K；15% PEG 6000, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 297.15 K	Resolution 2.20 Å R-free 0.283
3QFB Crystal structure of the human thioredoxin reductase-thioredoxin complex Deposited 2011-01-21	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–499（499 aa） Chain B 1–499（499 aa）	Mutation：C497S, U498C Mutation：C497S, U498C	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；297.15 K；15% PEG 4000, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 297.15K	Resolution 2.60 Å R-free 0.297
7X1R Cryo-EM structure of human thioredoxin reductase bound by Au Deposited 2022-02-24	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 152–649（498 aa） Chain B 152–649（498 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 AU GOLD ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
9UIN Human thioredoxin reductase 1 (SeCys 498 Cys) with Cu(I) Deposited 2025-04-15	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 151–649（499 aa） Chain B 151–649（499 aa）	Mutation：SEC498C Mutation：SEC498C	TXP 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 CU COPPER (II) ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å

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

View Construct and Data Evidence

UniProt name	TRXR1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 23–521； UniProt 1–499 Author chain B； PDBConstruct 23–521； UniProt 1–499 Author chain C； PDBConstruct 23–521； UniProt 1–499 Author chain D； PDBConstruct 23–521； UniProt 1–499 Author chain E； PDBConstruct 23–521； UniProt 1–499 Author chain F； PDBConstruct 23–521； UniProt 1–499

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	2cfy
Deposition date deposition_date	2006-02-26
Structure title title	Crystal structure of human thioredoxin reductase 1
Keywords keywords	OXIDOREDUCTASE, PHOSPHORYLATION, REDOX-ACTIVE CENTER, NADP; 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	55.80 Å
Radius of gyration Rg (electron density) rg_electron	56.56 Å
Forward intensity I(0) i0	1416470000.00
Molecular weight molecular_weight	316090.0 kDa
Excluded volume excluded_volume	396280 Å³
Envelope volume envelope_volume	552050 Å³
Hydration-shell volume shell_volume	87493 Å³
Envelope diameter envelope_diameter	216.2 Å
Shell Rg shell_rg	52.84 Å
Envelope Rg envelope_rg	55.69 Å
Shape Rg shape_rg	56.58 Å
Total Rg total_rg	56.39 Å
Total atoms total_atoms	22240
Residues n_residues	2904
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	199.3 Å
Rg (real space) rg_real	56.40 Å
Rg uncertainty (real space) rg_real_error	2.39 Å
I(0) (real space) i0_real	1.4160e+09
I(0) uncertainty (real space) i0_real_error	3.1190e+07
Rg (reciprocal space) rg_reciprocal	55.30 Å
I(0) (reciprocal space) i0_reciprocal	1414000000.0000
Solution quality estimate total_estimate	0.7928
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	49.8 Å
Skewness Skewness skewness	0.638
Kurtosis Kurtosis kurtosis	-0.139
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	180800000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.637; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.842; Smooth: 0.555

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	THIOREDOXIN REDUCTASE 1
Molecular weight formula_weight	57283.2 kDa
EC 编号 ec_number	1.8.1.9
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	22479

MHHHHHHSSGVDLGTENLYFQSMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCGG

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

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	6

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	228

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7. Fold Classification (SCOP + CATH) 18 domains

CATH v4.4 (18 domains)

Domain ID domain_id	2cfyA01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyA02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

Domain ID domain_id	2cfyB01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyB02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyB03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

Domain ID domain_id	2cfyC01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyC02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

Domain ID domain_id	2cfyD01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyD02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyD03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

Domain ID domain_id	2cfyE01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyE02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyE03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

Domain ID domain_id	2cfyF01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyF02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2cfyF03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

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8. Citations (1)

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Unit-cell length a length_a	89.756 Å
Unit-cell length b length_b	149.651 Å
Unit-cell length c length_c	146.789 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.96 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 1 2 1
Space-group number int_tables_number	3
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	149.070 Å
R factor r_factor	0.2050
R_work r_work	0.2030
R_free r_free	0.2480

fit	/app/data/saxs_computation/cf/2cfy/2cfy.fit
pddf	/app/data/pr_computation/cf/2cfy/2cfy.pr.out
profile	/app/data/saxs_computation/cf/2cfy/2cfy.dat