1w5g

An anti-parallel four helix bundle (acetimide modification).

Method: X-RAY DIFFRACTION Dmax: 56.7 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 249–281 Chain B; UniProt 249–281 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10;HANGING DROP, 1UL OF 1MG/ML PEPTIDE IN WATER, 1UL 100MM CAPS, 30% PEG 400, PH 10.5. Resolution 2.16 Å R-free 0.337

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 1–33; UniProt 249–281 Author chain B; PDBConstruct 1–33; 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 1w5g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1w5g
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1w5g
Deposition date deposition_date2004-08-06
Structure title titleAn anti-parallel four helix bundle (acetimide modification).
Keywords keywordsSTRUCTURAL PROTEIN, FOUR HELIX BUNDLE, ANTIPARALLEL FOUR HELIX BUNDLE; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.60
Radius of gyration Rg (electron density) rg_electron14.89
Forward intensity I(0) i0971719.00
Molecular weight molecular_weight7017.0 kDa
Excluded volume excluded_volume9060 ų
Envelope volume envelope_volume11063 ų
Hydration-shell volume shell_volume7388 ų
Envelope diameter envelope_diameter55.8
Shell Rg shell_rg18.25
Envelope Rg envelope_rg15.39
Shape Rg shape_rg14.87
Total Rg total_rg15.84
Total atoms total_atoms491
Residues n_residues65
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 dmax56.7
Rg (real space) rg_real15.81
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real9.7170e+05
I(0) uncertainty (real space) i0_real_error1.1190e+04
Rg (reciprocal space) rg_reciprocal15.79
I(0) (reciprocal space) i0_reciprocal971700.0000
Solution quality estimate total_estimate0.7021
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.3
Skewness Skewness skewness0.585
Kurtosis Kurtosis kurtosis-0.081
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76810.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.549; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.476; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1w5ga_
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_idd1w5gb_
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

8. Citations (1)

9. Files and Curves (10)