1yow

human Steroidogenic Factor 1 LBD with bound Co-factor Peptide

Method: X-RAY DIFFRACTION Dmax: 57.9 Å Quality: EXCELLENT

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

Steroidogenic factor 1

Homo sapiens

UniProt Q13285

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 222–461 Not recorded TIF2 peptide × 1 P0E PHOSPHATIDYL ETHANOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;0.1M NaCitrate pH5.6, 0.2M Li2SO4, 25% PEG3350, VAPOR DIFFUSION, HANGING DROP Resolution 3.00 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.

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

View Construct and Data Evidence
UniProt name STF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–242; UniProt 222–461

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 1yow

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yow
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1yow
Deposition date deposition_date2005-01-28
Structure title titlehuman Steroidogenic Factor 1 LBD with bound Co-factor Peptide
Keywords keywordsSteroidogenic factor 1, SF1, phospholipid, phosphatidyl ethanolamine, phosphatidyl glycerol, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.25
Radius of gyration Rg (electron density) rg_electron17.79
Forward intensity I(0) i012039600.00
Molecular weight molecular_weight27108.0 kDa
Excluded volume excluded_volume34493 ų
Envelope volume envelope_volume39767 ų
Hydration-shell volume shell_volume18610 ų
Envelope diameter envelope_diameter57.2
Shell Rg shell_rg24.02
Envelope Rg envelope_rg17.93
Shape Rg shape_rg17.79
Total Rg total_rg18.76
Total atoms total_atoms1902
Residues n_residues241
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 dmax57.9
Rg (real space) rg_real19.11
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.2040e+07
I(0) uncertainty (real space) i0_real_error1.2820e+05
Rg (reciprocal space) rg_reciprocal19.14
I(0) (reciprocal space) i0_reciprocal12040000.0000
Solution quality estimate total_estimate0.9038
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2291000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id1yowA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor

8. Citations (1)

9. Files and Curves (10)