2b1f

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat

Method: X-RAY DIFFRACTION Dmax: 56.9 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 251–281 Chain B; UniProt 251–281 Chain C; UniProt 251–281 Chain D; UniProt 251–281 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.2;295 K;Ethanol, Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K Resolution 1.50 Å R-free 0.283

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 4–34; UniProt 251–281 Author chain B; PDBConstruct 4–34; UniProt 251–281 Author chain C; PDBConstruct 4–34; UniProt 251–281 Author chain D; PDBConstruct 4–34; UniProt 251–281

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 2b1f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b1f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b1f
Deposition date deposition_date2005-09-15
Structure title titleAntiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat
Keywords keywordsCoiled coils, protein design, antiparallel tetramer, Ala coils, protein structure, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.00
Radius of gyration Rg (electron density) rg_electron15.52
Forward intensity I(0) i03560760.00
Molecular weight molecular_weight13921.0 kDa
Excluded volume excluded_volume17734 ų
Envelope volume envelope_volume20401 ų
Hydration-shell volume shell_volume11721 ų
Envelope diameter envelope_diameter54.8
Shell Rg shell_rg20.58
Envelope Rg envelope_rg16.12
Shape Rg shape_rg15.44
Total Rg total_rg16.77
Total atoms total_atoms980
Residues n_residues124
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 dmax56.9
Rg (real space) rg_real16.07
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real3.5610e+06
I(0) uncertainty (real space) i0_real_error4.5890e+04
Rg (reciprocal space) rg_reciprocal16.06
I(0) (reciprocal space) i0_reciprocal3561000.0000
Solution quality estimate total_estimate0.8122
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3
Skewness Skewness skewness0.522
Kurtosis Kurtosis kurtosis-0.013
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1204000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.567; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.890; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd2b1fa1
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_idd2b1fa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2b1fb2
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_idd2b1fb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2b1fc2
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_idd2b1fc3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2b1fd2
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_idd2b1fd3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)