5e69

Glucocorticoid receptor DNA binding domain - IL8 NF-kB response element complex

Method: X-RAY DIFFRACTION Dmax: 68.8 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 391–480 Chain B; UniProt 391–480 Fragment:unp residues 391-480 ;DNA (5'-D(*GP*AP*GP*GP*AP*AP*AP*TP*TP*CP*CP*AP*CP*GP*AP*T)-3') ; × 1 ;DNA (5'-D(*AP*TP*CP*GP*TP*GP*GP*AP*AP*TP*TP*TP*CP*CP*TP*C)-3') ; × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.1 M HEPES pH 7.5, 7.5% glycerol, 22% PEG 20000 Resolution 1.85 Å R-free 0.242

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 P04150-8
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–114; UniProt 391–480 Author chain B; PDBConstruct 25–114; UniProt 391–480

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 5e69

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5e69
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5e69
Deposition date deposition_date2015-10-09
Structure title titleGlucocorticoid receptor DNA binding domain - IL8 NF-kB response element complex
Keywords keywordsDNA binding proteins, dna binding protein-dna complex; dna binding protein/dna
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.88
Radius of gyration Rg (electron density) rg_electron19.47
Forward intensity I(0) i020044000.00
Molecular weight molecular_weight26290.0 kDa
Excluded volume excluded_volume29534 ų
Envelope volume envelope_volume37855 ų
Hydration-shell volume shell_volume17004 ų
Envelope diameter envelope_diameter69.0
Shell Rg shell_rg24.89
Envelope Rg envelope_rg19.61
Shape Rg shape_rg19.47
Total Rg total_rg20.08
Total atoms total_atoms1774
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 dmax68.8
Rg (real space) rg_real19.93
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real2.0040e+07
I(0) uncertainty (real space) i0_real_error2.8570e+05
Rg (reciprocal space) rg_reciprocal19.92
I(0) (reciprocal space) i0_reciprocal20040000.0000
Solution quality estimate total_estimate0.8617
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.184
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1926000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.928

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_id5e69A00
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_id5e69B00
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)