5emp

Transcription factor GRDBD and mmGRE complex

Method: X-RAY DIFFRACTION Dmax: 65.2 Å Quality: GOOD

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

Glucocorticoid receptor

Homo sapiens

UniProt P04150

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 411–500 Chain B; UniProt 411–500 Fragment:UNP RESIDUES 411-500 ;DNA (5'-D(*CP*CP*AP*GP*AP*AP*CP*AP*TP*GP*AP*TP*GP*TP*TP*CP*TP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*AP*GP*AP*AP*CP*AP*TP*(5CM)P*AP*TP*GP*TP*TP*CP*TP*G)-3') ; × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;50mM Tris, 200mM KCl, 50mM MgCl2, 10% PEG 4000 Resolution 2.30 Å R-free 0.238

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.

54 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–94; UniProt 411–500 Author chain B; PDBConstruct 5–94; UniProt 411–500

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 5emp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5emp
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5emp
Deposition date deposition_date2015-11-06
Structure title titleTranscription factor GRDBD and mmGRE complex
Keywords keywordsTranscription factor, complex, DNA, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.92
Radius of gyration Rg (electron density) rg_electron19.36
Forward intensity I(0) i021448900.00
Molecular weight molecular_weight26912.0 kDa
Excluded volume excluded_volume29976 ų
Envelope volume envelope_volume37802 ų
Hydration-shell volume shell_volume16990 ų
Envelope diameter envelope_diameter66.2
Shell Rg shell_rg24.62
Envelope Rg envelope_rg19.42
Shape Rg shape_rg19.35
Total Rg total_rg19.96
Total atoms total_atoms1811
Residues n_residues178
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 dmax65.2
Rg (real space) rg_real19.95
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.1450e+07
I(0) uncertainty (real space) i0_real_error3.1280e+05
Rg (reciprocal space) rg_reciprocal19.95
I(0) (reciprocal space) i0_reciprocal21450000.0000
Solution quality estimate total_estimate0.8928
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.3
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2164000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5empA00
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
Domain ID domain_id5empB00
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)