2ylp

TARGETING THE BINDING FUNCTION 3 SITE OF THE ANDROGEN RECEPTOR THROUGH IN SILICO MOLECULAR MODELING

Method: X-RAY DIFFRACTION Dmax: 61.6 Å Quality: GOOD

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

ANDROGEN RECEPTOR

HOMO SAPIENS

UniProt P10275

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 664–919 Fragment:LIGAND-BINDING DOMAIN, RESIDUES 664-919 SO4 SULFATE ION × 1 TES TESTOSTERONE × 1 056 3-[(2,4-DICHLOROPHENYL)METHYLSULFANYLMETHYL]BENZOIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 2.30 Å R-free 0.249

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.

94 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANDR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–256; UniProt 664–919

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 2ylp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ylp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ylp
Deposition date deposition_date2011-06-04
Structure title titleTARGETING THE BINDING FUNCTION 3 SITE OF THE ANDROGEN RECEPTOR THROUGH IN SILICO MOLECULAR MODELING
Keywords keywordsHORMONE RECEPTOR, BINDING FUNCTION 3; HORMONE RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.11
Radius of gyration Rg (electron density) rg_electron18.10
Forward intensity I(0) i027251900.00
Molecular weight molecular_weight27466.0 kDa
Excluded volume excluded_volume26905 ų
Envelope volume envelope_volume41558 ų
Hydration-shell volume shell_volume19158 ų
Envelope diameter envelope_diameter66.4
Shell Rg shell_rg24.50
Envelope Rg envelope_rg18.33
Shape Rg shape_rg18.03
Total Rg total_rg18.90
Total atoms total_atoms2069
Residues n_residues249
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 dmax61.6
Rg (real space) rg_real19.02
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.7250e+07
I(0) uncertainty (real space) i0_real_error3.0390e+05
Rg (reciprocal space) rg_reciprocal19.03
I(0) (reciprocal space) i0_reciprocal27250000.0000
Solution quality estimate total_estimate0.8091
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.0
Skewness Skewness skewness0.237
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5362000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.838; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2ylpa_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain

CATH v4.4 (1 domains)

Domain ID domain_id2ylpA00
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)