3gjp

Crystal structure of mutant coiled coil GCN4 leucine zipper

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: GOOD

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

General control protein GCN4

Saccharomyces cerevisiae

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 Chain B; UniProt 249–281 Chain C; UniProt 249–281 Fragment:Leucine zipper Mutation:V271I,L274I No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.269

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 3–35; UniProt 249–281 Author chain B; PDBConstruct 3–35; UniProt 249–281 Author chain C; PDBConstruct 3–35; 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 3gjp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3gjp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3gjp
Deposition date deposition_date2009-03-09
Structure title titleCrystal structure of mutant coiled coil GCN4 leucine zipper
Keywords keywords;Transcription regulation, nuclear protein, DNA-binding, amino-acid biosynthesis, activator, trimeric coiled coil, trigger site, nucleus, phosphoprotein, transcription ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.39
Radius of gyration Rg (electron density) rg_electron16.49
Forward intensity I(0) i03122950.00
Molecular weight molecular_weight12293.0 kDa
Excluded volume excluded_volume15417 ų
Envelope volume envelope_volume19027 ų
Hydration-shell volume shell_volume10787 ų
Envelope diameter envelope_diameter59.1
Shell Rg shell_rg20.60
Envelope Rg envelope_rg16.96
Shape Rg shape_rg16.41
Total Rg total_rg17.53
Total atoms total_atoms861
Residues n_residues103
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 dmax59.9
Rg (real space) rg_real17.55
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real3.1230e+06
I(0) uncertainty (real space) i0_real_error4.3430e+04
Rg (reciprocal space) rg_reciprocal17.53
I(0) (reciprocal space) i0_reciprocal3123000.0000
Solution quality estimate total_estimate0.8169
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.6
Skewness Skewness skewness0.562
Kurtosis Kurtosis kurtosis-0.181
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha701600.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.624; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)