2wpy

GCN4 leucine zipper mutant with one VxxNxxx motif coordinating chloride

Method: X-RAY DIFFRACTION Dmax: 52.2 Å Quality: REASONABLE

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

GENERAL CONTROL PROTEIN GCN4

OrganismNot specified

UniProt P03069

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 249–281 Fragment:COILED-COIL DOMAIN, RESIDUES 249-281 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:3.2 M NACL, 100 MM NA-ACETATE, PH 4.6 Resolution 1.75 Å R-free 0.252

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.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–34; UniProt 249–281

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 2wpy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wpy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2wpy
Deposition date deposition_date2009-08-12
Structure title titleGCN4 leucine zipper mutant with one VxxNxxx motif coordinating chloride
Keywords keywords;AMINO-ACID BIOSYNTHESIS, TRANSCRIPTION REGULATION, ION COORDINATION, POLAR CORE RESIDUES, TRANSCRIPTION, PROTEIN EXPORT, PHOSPHOPROTEIN, TAA, NUCLEUS, ACTIVATOR, DNA-BINDING, TRIMERIC AUTOTRANSPORTER ADHESIN ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.11
Radius of gyration Rg (electron density) rg_electron14.23
Forward intensity I(0) i0392581.00
Molecular weight molecular_weight3879.0 kDa
Excluded volume excluded_volume4866 ų
Envelope volume envelope_volume6301 ų
Hydration-shell volume shell_volume4890 ų
Envelope diameter envelope_diameter49.9
Shell Rg shell_rg16.44
Envelope Rg envelope_rg14.72
Shape Rg shape_rg14.18
Total Rg total_rg15.01
Total atoms total_atoms269
Residues n_residues32
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 dmax52.2
Rg (real space) rg_real14.50
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real3.9260e+05
I(0) uncertainty (real space) i0_real_error5.2880e+03
Rg (reciprocal space) rg_reciprocal14.47
I(0) (reciprocal space) i0_reciprocal392600.0000
Solution quality estimate total_estimate0.7290
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.9
Skewness Skewness skewness0.671
Kurtosis Kurtosis kurtosis-0.225
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26640.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.489; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.055; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)