5emc

Transcription factor GRDBD and smGRE complex

Method: X-RAY DIFFRACTION Dmax: 63.7 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*(5CM)P*AP*TP*CP*AP*TP*GP*TP*TP*(5CM)P*TP*G)-3') ; × 1 ;DNA (5'-D(*CP*CP*AP*GP*AP*AP*(5CM)P*AP*TP*GP*AP*TP*GP*TP*TP*(5CM)P*TP*G)-3') ; × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;50mM HEPES, 100mM KCl, 10mM MgCl2, 5% PEG 400 Resolution 2.30 Å R-free 0.261

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 2
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 5emc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5emc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5emc
Deposition date deposition_date2015-11-06
Structure title titleTranscription factor GRDBD and smGRE 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_guinier19.74
Radius of gyration Rg (electron density) rg_electron19.28
Forward intensity I(0) i020865800.00
Molecular weight molecular_weight26560.0 kDa
Excluded volume excluded_volume29594 ų
Envelope volume envelope_volume37096 ų
Hydration-shell volume shell_volume16789 ų
Envelope diameter envelope_diameter65.2
Shell Rg shell_rg24.50
Envelope Rg envelope_rg19.33
Shape Rg shape_rg19.27
Total Rg total_rg19.87
Total atoms total_atoms1789
Residues n_residues174
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 dmax63.7
Rg (real space) rg_real19.76
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real2.0870e+07
I(0) uncertainty (real space) i0_real_error2.5820e+05
Rg (reciprocal space) rg_reciprocal19.76
I(0) (reciprocal space) i0_reciprocal20870000.0000
Solution quality estimate total_estimate0.8991
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2134000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.997

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_id5emcA00
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_id5emcB00
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)