SAXSdb — 1ekg

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

FRATAXIN

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 84–210	Fragment：RESIDUES 88-210	No other associated polymer	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

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 1EKG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
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 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 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 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 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 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 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 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 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 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 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 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 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 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 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
9HO4 Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 6B1 Deposited 2024-12-11	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 93–206（114 aa）	Not recorded	No recorded non-water small molecule	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
9HO5 Crystal Structure of the Human Frataxin protein in complex with a tailored Camelid Nanobody 4A7 Deposited 2024-12-11	Different construct Different oligomeric state 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 oligomeric state 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 oligomeric state 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 1–127； UniProt 84–210

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	1ekg
Deposition date deposition_date	2000-03-08
Structure title title	MATURE HUMAN FRATAXIN
Keywords keywords	;Freidreich's ataxia, iron transport, mitochondrial, disease, METAL TRANSPORT ;; METAL TRANSPORT
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	15.34 Å
Radius of gyration Rg (electron density) rg_electron	13.89 Å
Forward intensity I(0) i0	3400580.00
Molecular weight molecular_weight	13264.0 kDa
Excluded volume excluded_volume	16712 Å³
Envelope volume envelope_volume	18765 Å³
Hydration-shell volume shell_volume	11681 Å³
Envelope diameter envelope_diameter	49.7 Å
Shell Rg shell_rg	19.43 Å
Envelope Rg envelope_rg	14.22 Å
Shape Rg shape_rg	13.87 Å
Total Rg total_rg	15.15 Å
Total atoms total_atoms	940
Residues n_residues	119
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	50.2 Å
Rg (real space) rg_real	15.26 Å
Rg uncertainty (real space) rg_real_error	0.27 Å
I(0) (real space) i0_real	3.4010e+06
I(0) uncertainty (real space) i0_real_error	3.6790e+04
Rg (reciprocal space) rg_reciprocal	15.27 Å
I(0) (reciprocal space) i0_reciprocal	3401000.0000
Solution quality estimate total_estimate	0.8782
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.1 Å
Skewness Skewness skewness	0.223
Kurtosis Kurtosis kurtosis	-0.230
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	574200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.990

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ekga_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.82 — N domain of copper amine oxidase-like
Superfamily Superfamily superfamily	d.82.2 — Frataxin/Nqo15-like
Family Family family	d.82.2.1 — Frataxin-like

CATH v4.4 (1 domains)

Domain ID domain_id	1ekgA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	920 — Metal Transport, Frataxin; Chain A
Homologous superfamily homologous superfamily	10 — Frataxin/CyaY

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8. Citations (1)

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Unit-cell length a length_a	44.050 Å
Unit-cell length b length_b	45.220 Å
Unit-cell length c length_c	68.950 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1970
R_work r_work	0.1970
R_free r_free	0.2200

Description description	FRATAXIN
Molecular weight formula_weight	14045.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1021

MATURE HUMAN FRATAXIN

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

FRATAXIN

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	81

fit	/app/data/saxs_computation/ek/1ekg/1ekg.fit
pddf	/app/data/pr_computation/ek/1ekg/1ekg.pr.out
profile	/app/data/saxs_computation/ek/1ekg/1ekg.dat