7xe4

structure of a membrane-bound glycosyltransferase

Method: ELECTRON MICROSCOPY Dmax: 129.0 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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 1–1876 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 DD9 nonane × 7 D10 DECANE × 6 C14 TETRADECANE × 1 HP6 HEPTANE × 7 D12 DODECANE × 3 XKP (11R,14S)-17-amino-14-hydroxy-8,14-dioxo-9,13,15-trioxa-14lambda~5~-phosphaheptadecan-11-yl decanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 F; PDBConstruct 1–1876; UniProt 1–1876

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 7xe4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xe4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7xe4
Deposition date deposition_date2022-03-29
Structure title titlestructure of a membrane-bound glycosyltransferase
Keywords keywordsmembrane protein, glycosyltransferase, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.99
Radius of gyration Rg (electron density) rg_electron39.23
Forward intensity I(0) i0403391000.00
Molecular weight molecular_weight177550.0 kDa
Excluded volume excluded_volume228110 ų
Envelope volume envelope_volume328090 ų
Hydration-shell volume shell_volume68013 ų
Envelope diameter envelope_diameter133.2
Shell Rg shell_rg46.60
Envelope Rg envelope_rg38.54
Shape Rg shape_rg39.18
Total Rg total_rg39.90
Total atoms total_atoms12529
Residues n_residues1503
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 dmax129.0
Rg (real space) rg_real39.89
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real4.0340e+08
I(0) uncertainty (real space) i0_real_error6.7320e+06
Rg (reciprocal space) rg_reciprocal39.99
I(0) (reciprocal space) i0_reciprocal403400000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.4
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.448
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha71560000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)