9pe2

Structure of beta-1,3-glucan synthase from Saccharomyces cerevisiae (ScFks1) in complex with short glucan

Method: ELECTRON MICROSCOPY Dmax: 129.2 Å Quality: GOOD

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

1,3-beta-glucan synthase component FKS1

OrganismNot specified

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 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1876 Not recorded Gsr1p × 1 (Q03559) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 29 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 UDP URIDINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 A; PDBConstruct 1–1876; UniProt 1–1876

Gsr1p

OrganismNot specified

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 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–197 Not recorded 1,3-beta-glucan synthase component FKS1 × 1 (P38631) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 29 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 UDP URIDINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 G; 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 9pe2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pe2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pe2
Deposition date deposition_date2025-07-01
Structure title titleStructure of beta-1,3-glucan synthase from Saccharomyces cerevisiae (ScFks1) in complex with short glucan
Keywords keywordsEnzyme, glucan synthesis, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.79
Radius of gyration Rg (electron density) rg_electron38.31
Forward intensity I(0) i0513001000.00
Molecular weight molecular_weight207510.0 kDa
Excluded volume excluded_volume268440 ų
Envelope volume envelope_volume330400 ų
Hydration-shell volume shell_volume68878 ų
Envelope diameter envelope_diameter130.7
Shell Rg shell_rg46.28
Envelope Rg envelope_rg38.58
Shape Rg shape_rg38.28
Total Rg total_rg38.87
Total atoms total_atoms29312
Residues n_residues1695
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 dmax129.2
Rg (real space) rg_real38.73
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real5.1300e+08
I(0) uncertainty (real space) i0_real_error9.0710e+06
Rg (reciprocal space) rg_reciprocal38.77
I(0) (reciprocal space) i0_reciprocal513000000.0000
Solution quality estimate total_estimate0.8794
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94640000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)