3s5d

Crystal structure of human frataxin variant W155A

Method: X-RAY DIFFRACTION Dmax: 48.2 Å Quality: GOOD

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

Frataxin, mitochondrial

Homo sapiens

UniProt Q16595

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 82–210 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

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.

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 1–129; UniProt 82–210

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3s5d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3s5d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3s5d
Deposition date deposition_date2011-05-23
Structure title titleCrystal structure of human frataxin variant W155A
Keywords keywordsallosteric activator, mitochondrion, alpha beta 2-layer sandwich, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.38
Radius of gyration Rg (electron density) rg_electron13.88
Forward intensity I(0) i03589070.00
Molecular weight molecular_weight13430.0 kDa
Excluded volume excluded_volume16812 ų
Envelope volume envelope_volume18548 ų
Hydration-shell volume shell_volume11604 ų
Envelope diameter envelope_diameter47.0
Shell Rg shell_rg19.32
Envelope Rg envelope_rg14.13
Shape Rg shape_rg13.85
Total Rg total_rg15.09
Total atoms total_atoms949
Residues n_residues121
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax48.2
Rg (real space) rg_real15.29
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real3.5890e+06
I(0) uncertainty (real space) i0_real_error3.5930e+04
Rg (reciprocal space) rg_reciprocal15.30
I(0) (reciprocal space) i0_reciprocal3589000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.320
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha530500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3s5da_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.82 — N domain of copper amine oxidase-like
Superfamily Superfamily superfamilyd.82.2 — Frataxin/Nqo15-like
Family Family familyd.82.2.1 — Frataxin-like

CATH v4.4 (1 domains)

Domain ID domain_id3s5dA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology920 — Metal Transport, Frataxin; Chain A
Homologous superfamily homologous superfamily10 — Frataxin/CyaY

8. Citations (1)

9. Files and Curves (10)