SAXSdb — 9ho4

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

Frataxin mature form

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 93–206	Not recorded	Camelid Nanobody 6B1 × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；291 K；0.1M HEPES pH 7.0 0.8M Potassium Sodium Tartrate	Resolution 1.76 Å R-free 0.175

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 9HO4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EKG MATURE HUMAN FRATAXIN Deposited 2000-03-08	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 84–210（127 aa） Fragment：RESIDUES 88-210	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；2.5 M ammonium sulfate, 0.1 sodium citrate, 2% sucrose, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K	Resolution 1.80 Å R-free 0.220
1LY7 The solution structure of the the c-terminal domain of frataxin, the protein responsible for friedreich ataxia Deposited 2002-06-07	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 91–210（120 aa） Fragment：C-TERMINAL DOMAIN (91-210)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；300 K；Ionic strength (raw mmCIF value) 10 mM phosphate；Pressure ambient NMR sample composition 1 MM FRATAXIN. U-15N 10 MM PHOSPHATE BUFFER (PH 6.8)90% H2O, 10% D2O \| h2o	Resolution not provided
3S4M Crystal structure of wild-type human frataxin Deposited 2011-05-19	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；295 K；30% MPD, 0.1 M sodium citrate, 0.2 M ammonium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.30 Å R-free 0.187
3S5D Crystal structure of human frataxin variant W155A Deposited 2011-05-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：W155A	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；295 K；1.8 M ammonium sulfate, 0.2 M potassium sodium tartrate tetrahydrate, 0.1 M sodium citrate tribasic dihydrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.50 Å R-free 0.192
3S5E Crystal structure of human frataxin variant W155R, one of the Friedreich's ataxia point mutations Deposited 2011-05-23	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：W155R	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；16% PEG2000 MME, 0.1 M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.31 Å R-free 0.197
3S5F Crystal structure of human frataxin variant W155F Deposited 2011-05-23	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：W155F	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.2 M sodium acetate trihydrate, 0.1 M Tris hydrochloride, 30% PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.50 Å R-free 0.213
3S5F Crystal structure of human frataxin variant W155F Deposited 2011-05-23	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：W155F	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.2 M sodium acetate trihydrate, 0.1 M Tris hydrochloride, 30% PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.50 Å R-free 0.213
3T3J 1.70 A structure of Friedreich's ataxia frataxin variant N146K Deposited 2011-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：N146K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；28% PEG2000 MME, 0.1 M Tris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.245
3T3K 1.24 A Structure of Friedreich's ataxia frataxin variant Q148R Deposited 2011-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：Q148R	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；20% PEG3000, 0.1 M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.24 Å R-free 0.197
3T3L 1.15 A structure of human frataxin variant Q153A Deposited 2011-07-25	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：Q153A	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；295 K；2.0 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, 0.2 M potassium sodium tartrate tetrahydrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.15 Å R-free 0.179
3T3T 1.38 A structure of human frataxin variant Q148G Deposited 2011-07-25	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：Q148G	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；2.0 M ammonium sulfate, 0.1 M citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.38 Å R-free 0.227
3T3T 1.38 A structure of human frataxin variant Q148G Deposited 2011-07-25	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：Q148G	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；2.0 M ammonium sulfate, 0.1 M citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.38 Å R-free 0.227
3T3T 1.38 A structure of human frataxin variant Q148G Deposited 2011-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：Q148G	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；2.0 M ammonium sulfate, 0.1 M citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.38 Å R-free 0.227
3T3T 1.38 A structure of human frataxin variant Q148G Deposited 2011-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：Q148G	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；2.0 M ammonium sulfate, 0.1 M citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.38 Å R-free 0.227
3T3X 1.57 A structure of Friedreich's ataxia frataxin variant R165C Deposited 2011-07-25	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：R165C	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；1.9 M ammonium sulfate, 0.1 M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.57 Å R-free 0.251
3T3X 1.57 A structure of Friedreich's ataxia frataxin variant R165C Deposited 2011-07-25	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 82–210（129 aa） Fragment：mature form (UNP residues 82-210)	Mutation：R165C	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；1.9 M ammonium sulfate, 0.1 M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.57 Å R-free 0.251
5KZ5 Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly Machinery: the Complex Formed by the Iron Donor, the Sulfur Donor, and the Scaffold Deposited 2016-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain A 42–210（169 aa） Chain B 42–210（169 aa） Chain C 42–210（169 aa） Chain D 42–210（169 aa） Chain E 42–210（169 aa） Chain F 42–210（169 aa） Chain G 42–210（169 aa） Chain H 42–210（169 aa） Chain I 42–210（169 aa） Chain J 42–210（169 aa） Chain K 42–210（169 aa） Chain L 42–210（169 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8	Resolution 14.30 Å
6NZU Structure of the human frataxin-bound iron-sulfur cluster assembly complex Deposited 2019-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain I 81–210（130 aa） Fragment：UNP residues 81-210 Chain J 81–210（130 aa） Fragment：UNP residues 81-210	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8PK8 Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during persulfide transfer (persulfide on ISCU2) Deposited 2023-06-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 81–210（130 aa）	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 FE2 FE (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
8PK9 Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during persulfide transfer (persulfide on NFS1 and ISCU2) Deposited 2023-06-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 81–210（130 aa）	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 FE2 FE (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.58 Å
8RME Structure of the core ISC complex under turnover conditions (frataxin-bound) Deposited 2024-01-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain I 81–210（130 aa）	Not recorded	FE2 FE (II) ION × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
9HO5 Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 4A7 Deposited 2024-12-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 90–210（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Sodium Thiocyanate pH 6.9 20% PEG 3350	Resolution 1.50 Å R-free 0.210
9HO6 Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 16C10 Deposited 2024-12-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 90–210（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；15% PEG 10K 0.1M Ammonium acetate 0.1M Bis-Tris pH 5.5	Resolution 2.00 Å R-free 0.227
9HO6 Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 16C10 Deposited 2024-12-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 90–210（121 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；15% PEG 10K 0.1M Ammonium acetate 0.1M Bis-Tris pH 5.5	Resolution 2.00 Å R-free 0.227

18 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FRDA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–114； UniProt 93–206

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	9ho4
Deposition date deposition_date	2024-12-11
最后修订 last_revision	2025-12-24
Structure title title	Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 6B1
Keywords keywords	Complex, Nanobody, Mitochondrial Regulation, Friedreich Ataxia, OXIDOREDUCTASE; 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	21.28 Å
Radius of gyration Rg (electron density) rg_electron	20.57 Å
Forward intensity I(0) i0	12743200.00
Molecular weight molecular_weight	26522.0 kDa
Excluded volume excluded_volume	33084 Å³
Envelope volume envelope_volume	38821 Å³
Hydration-shell volume shell_volume	16937 Å³
Envelope diameter envelope_diameter	76.8 Å
Shell Rg shell_rg	25.70 Å
Envelope Rg envelope_rg	20.82 Å
Shape Rg shape_rg	20.57 Å
Total Rg total_rg	21.33 Å
Total atoms total_atoms	1875
Residues n_residues	242
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	75.6 Å
Rg (real space) rg_real	21.38 Å
Rg uncertainty (real space) rg_real_error	0.56 Å
I(0) (real space) i0_real	1.2740e+07
I(0) uncertainty (real space) i0_real_error	1.6290e+05
Rg (reciprocal space) rg_reciprocal	21.36 Å
I(0) (reciprocal space) i0_reciprocal	12740000.0000
Solution quality estimate total_estimate	0.8338
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.1 Å
Skewness Skewness skewness	0.442
Kurtosis Kurtosis kurtosis	-0.355
Angular range angular_range	— – 0.3750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4040000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.693; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.771; Smooth: 0.984

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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	Frataxin mature form
Molecular weight formula_weight	12758.1 kDa
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	2042

TTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYS

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

Entity 2 Entity 2 polymer

Description description	Camelid Nanobody 6B1
Molecular weight formula_weight	13827.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

VQLQESGGGLVQPGGSLRLSCAASGSIFSTDAMGWYRQFPGKNRKLVARISSGDYGDYTNYADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCNSVPPAPGEYGRDYWGAGTQVTVSSAAAYPY

来源 Source

来源生物 organism	Lama glama
通用名 common_name	llama
NCBI Class编号 ncbi_taxonomy_id	9844
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	153

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8. Citations (1)

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Unit-cell length a length_a	97.253 Å
Unit-cell length b length_b	97.253 Å
Unit-cell length c length_c	128.105 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	12

Space group space_group	P 63 2 2
Space-group number int_tables_number	182
Crystal system crystal_system	hexagonal

Resolution resolution	1.760 Å
Low-resolution limit resolution_low	84.224 Å
R factor r_factor	—
R_work r_work	0.1509
R_free r_free	0.1753

fit	/app/data/saxs_computation/ho/9ho4/9ho4.fit
pddf	/app/data/pr_computation/ho/9ho4/9ho4.pr.out
profile	/app/data/saxs_computation/ho/9ho4/9ho4.dat

Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 6B1

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

Frataxin mature form

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)