1rxr

HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE

Method: SOLUTION NMR Dmax: 46.6 Å Quality: GOOD

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

RETINOIC ACID RECEPTOR-ALPHA

Homo sapiens

UniProt P19793

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 130–212 Fragment:DNA-BINDING DOMAIN, 130-212 Mutation:C195A ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.6;300 K;Ionic strength (raw mmCIF value) 120;Pressure AMBIENT NMR sample composition:WATER Resolution not provided

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.

107 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RXRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–83; UniProt 130–212

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 1rxr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rxr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rxr
Deposition date deposition_date1998-06-12
Structure title titleHIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE
Keywords keywordsTRANSCRIPTION FACTOR, NUCLEAR HORMONE RECEPTOR, ZINC-FINGER; TRANSCRIPTION FACTOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.77
Radius of gyration Rg (electron density) rg_electron12.79
Forward intensity I(0) i0680472000.00
Molecular weight molecular_weight198400.0 kDa
Excluded volume excluded_volume239600 ų
Envelope volume envelope_volume24137 ų
Hydration-shell volume shell_volume13458 ų
Envelope diameter envelope_diameter54.5
Shell Rg shell_rg21.14
Envelope Rg envelope_rg15.88
Shape Rg shape_rg12.82
Total Rg total_rg12.86
Total atoms total_atoms27000
Residues n_residues1660
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 dmax46.6
Rg (real space) rg_real12.76
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real6.8050e+08
I(0) uncertainty (real space) i0_real_error9.2780e+06
Rg (reciprocal space) rg_reciprocal12.76
I(0) (reciprocal space) i0_reciprocal680500000.0000
Solution quality estimate total_estimate0.7703
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.8
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha173000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.860; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1rxra_
Class classg — Small proteins
Fold Fold foldg.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamilyg.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family familyg.39.1.2 — Nuclear receptor

CATH v4.4 (1 domains)

Domain ID domain_id1rxrA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A

8. Citations (1)

9. Files and Curves (10)