5kht

Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution

Method: X-RAY DIFFRACTION Dmax: 76.6 Å Quality: REASONABLE

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

Tropomyosin alpha-1 chain,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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 264–281 Chain C; UniProt 264–281 Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;PEG 8000, Hepes/sodium hydroxide Resolution 1.50 Å R-free 0.249
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 264–281 Chain D; UniProt 264–281 Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;PEG 8000, Hepes/sodium hydroxide Resolution 1.50 Å R-free 0.249

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 30–47; UniProt 264–281 Author chain B; PDBConstruct 30–47; UniProt 264–281 Author chain C; PDBConstruct 30–47; UniProt 264–281 Author chain D; PDBConstruct 30–47; UniProt 264–281

Tropomyosin alpha-1 chain,General control protein GCN4

Saccharomyces cerevisiae

UniProt P09493

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 1–28 Chain C; UniProt 1–28 Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;PEG 8000, Hepes/sodium hydroxide Resolution 1.50 Å R-free 0.249
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–28 Chain D; UniProt 1–28 Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;PEG 8000, Hepes/sodium hydroxide Resolution 1.50 Å R-free 0.249

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPM1_HUMAN
Isoform P09493-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–29; UniProt 1–28 Author chain B; PDBConstruct 2–29; UniProt 1–28 Author chain C; PDBConstruct 2–29; UniProt 1–28 Author chain D; PDBConstruct 2–29; UniProt 1–28

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 5kht

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5kht
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5kht
Deposition date deposition_date2016-06-15
Structure title titleCrystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution
Keywords keywordstropomyosin, coiled coil, actin-binding protein; actin-binding protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.05
Radius of gyration Rg (electron density) rg_electron22.98
Forward intensity I(0) i09516250.00
Molecular weight molecular_weight22126.0 kDa
Excluded volume excluded_volume27489 ų
Envelope volume envelope_volume38264 ų
Hydration-shell volume shell_volume14930 ų
Envelope diameter envelope_diameter76.7
Shell Rg shell_rg28.06
Envelope Rg envelope_rg23.27
Shape Rg shape_rg22.80
Total Rg total_rg24.25
Total atoms total_atoms1540
Residues n_residues187
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 dmax76.6
Rg (real space) rg_real23.11
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real9.5160e+06
I(0) uncertainty (real space) i0_real_error1.2450e+05
Rg (reciprocal space) rg_reciprocal23.10
I(0) (reciprocal space) i0_reciprocal9516000.0000
Solution quality estimate total_estimate0.7393
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.287
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha571500.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 0.307; Positv: 1.000; Valcen: 0.885; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5khtA00
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 superfamily1160 — Vasodilator-stimulated phosphoprotein
Domain ID domain_id5khtB00
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 superfamily1160 — Vasodilator-stimulated phosphoprotein
Domain ID domain_id5khtC00
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 superfamily1160 — Vasodilator-stimulated phosphoprotein
Domain ID domain_id5khtD00
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 superfamily1160 — Vasodilator-stimulated phosphoprotein

8. Citations (1)

9. Files and Curves (10)