1hbw

Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)

Method: SOLUTION NMR Dmax: 86.3 Å Quality: REASONABLE

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

REGULATORY PROTEIN GAL4

OrganismNot specified

UniProt P04386

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 50–106 Chain B; UniProt 50–106 Fragment:DIMERIZATION DOMAIN RESIDUES 50-106 Mutation:YES No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;308 K;Ionic strength (raw mmCIF value) 50 MM SODIUM PHOSPHATE 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GAL4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–57; UniProt 50–106 Author chain B; PDBConstruct 1–57; UniProt 50–106

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 1hbw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hbw
Deposition date deposition_date2001-04-20
Structure title titleSolution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)
Keywords keywordsTRANSCRIPTIONAL ACTIVATOR, GALACTOSE AND MELIBIOSE METABOLISM, DIMERIZATION DOMAIN, COILED-COIL DIMERIC; TRANSCRIPTIONAL ACTIVATOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier23.80
Radius of gyration Rg (electron density) rg_electron23.39
Forward intensity I(0) i0705941000.00
Molecular weight molecular_weight227140.0 kDa
Excluded volume excluded_volume286320 ų
Envelope volume envelope_volume72611 ų
Hydration-shell volume shell_volume23700 ų
Envelope diameter envelope_diameter92.9
Shell Rg shell_rg33.03
Envelope Rg envelope_rg27.88
Shape Rg shape_rg23.41
Total Rg total_rg23.57
Total atoms total_atoms32334
Residues n_residues1938
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 dmax86.3
Rg (real space) rg_real24.30
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real7.0590e+08
I(0) uncertainty (real space) i0_real_error1.0520e+07
Rg (reciprocal space) rg_reciprocal24.18
I(0) (reciprocal space) i0_reciprocal705900000.0000
Solution quality estimate total_estimate0.7221
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.2
Skewness Skewness skewness0.582
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha335800.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.451; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.092; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hbwa_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1hbwb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain

CATH v4.4 (2 domains)

Domain ID domain_id1hbwA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1hbwB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170

8. Citations (1)

9. Files and Curves (10)