2efs

Crystal structure of the C-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 2.0 angstroms resolution

Method: X-RAY DIFFRACTION Dmax: 217.2 Å Quality: REASONABLE

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

General control protein GCN4 and Tropomyosin 1 alpha chain

Oryctolagus cuniculus

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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 249–277 Chain B; UniProt 249–277 Fragment:residues 147-175, residues 176-301 Mutation:C190S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;40% MPD, 0.4M AMMONIUM ACETATE 0.1M TRIS-HCL, pH 8.50, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.00 Å R-free 0.304
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 249–277 Chain D; UniProt 249–277 Fragment:residues 147-175, residues 176-301 Mutation:C190S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;40% MPD, 0.4M AMMONIUM ACETATE 0.1M TRIS-HCL, pH 8.50, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.00 Å R-free 0.304

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 199 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 1–29; UniProt 249–277 Author chain B; PDBConstruct 1–29; UniProt 249–277 Author chain C; PDBConstruct 1–29; UniProt 249–277 Author chain D; PDBConstruct 1–29; UniProt 249–277

General control protein GCN4 and Tropomyosin 1 alpha chain

Oryctolagus cuniculus

UniProt P58772

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 176–273 Chain B; UniProt 176–273 Fragment:residues 147-175, residues 176-301 Mutation:C190S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;40% MPD, 0.4M AMMONIUM ACETATE 0.1M TRIS-HCL, pH 8.50, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.00 Å R-free 0.304
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 176–273 Chain D; UniProt 176–273 Fragment:residues 147-175, residues 176-301 Mutation:C190S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;40% MPD, 0.4M AMMONIUM ACETATE 0.1M TRIS-HCL, pH 8.50, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.00 Å R-free 0.304

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.

10 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPM1_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 30–127; UniProt 176–273 Author chain B; PDBConstruct 30–127; UniProt 176–273 Author chain C; PDBConstruct 30–127; UniProt 176–273 Author chain D; PDBConstruct 30–127; UniProt 176–273

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 2efs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2efs
Deposition date deposition_date2007-02-23
Structure title titleCrystal structure of the C-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 2.0 angstroms resolution
Keywords keywordsDESTABILIZING CLUSTER, HYDROPHOBIC CORE, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier64.95
Radius of gyration Rg (electron density) rg_electron68.32
Forward intensity I(0) i078467000.00
Molecular weight molecular_weight72554.0 kDa
Excluded volume excluded_volume90902 ų
Envelope volume envelope_volume163240 ų
Hydration-shell volume shell_volume25687 ų
Envelope diameter envelope_diameter238.9
Shell Rg shell_rg46.30
Envelope Rg envelope_rg67.50
Shape Rg shape_rg68.21
Total Rg total_rg67.89
Total atoms total_atoms5096
Residues n_residues616
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 dmax217.2
Rg (real space) rg_real66.72
Rg uncertainty (real space) rg_real_error2.37
I(0) (real space) i0_real7.8400e+07
I(0) uncertainty (real space) i0_real_error1.8590e+06
Rg (reciprocal space) rg_reciprocal63.23
I(0) (reciprocal space) i0_reciprocal77960000.0000
Solution quality estimate total_estimate0.6867
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.3
Skewness Skewness skewness0.616
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0012
Highest regularization parameter α highest_alpha5644000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.423; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.449; Smooth: 0.216

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2efsA00
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_id2efsB00
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_id2efsC00
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_id2efsD00
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)