9utu

Structure of Fks1 in complex with YMR295C

Method: ELECTRON MICROSCOPY Dmax: 130.3 Å Quality: GOOD

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

1,3-beta-glucan synthase component FKS1

Saccharomyces cerevisiae

UniProt P38631

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–1876 Not recorded YMR295C isoform 1 × 1 (Q03559) MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 Å

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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FKS1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–1876; UniProt 1–1876

YMR295C isoform 1

Saccharomyces cerevisiae

UniProt Q03559

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–197 Not recorded 1,3-beta-glucan synthase component FKS1 × 1 (P38631) MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 Å

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YM8V_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–197; UniProt 1–197

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 9utu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9utu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9utu
Deposition date deposition_date2025-05-05
Structure title titleStructure of Fks1 in complex with YMR295C
Keywords keywordsMEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.08
Radius of gyration Rg (electron density) rg_electron39.52
Forward intensity I(0) i0391539000.00
Molecular weight molecular_weight169850.0 kDa
Excluded volume excluded_volume216190 ų
Envelope volume envelope_volume321120 ų
Hydration-shell volume shell_volume66658 ų
Envelope diameter envelope_diameter131.2
Shell Rg shell_rg46.45
Envelope Rg envelope_rg38.52
Shape Rg shape_rg39.48
Total Rg total_rg40.12
Total atoms total_atoms11987
Residues n_residues1470
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 dmax130.3
Rg (real space) rg_real39.97
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real3.9150e+08
I(0) uncertainty (real space) i0_real_error6.2470e+06
Rg (reciprocal space) rg_reciprocal40.08
I(0) (reciprocal space) i0_reciprocal391600000.0000
Solution quality estimate total_estimate0.8963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.8
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70690000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)