9op1

Cryo-EM structure of Candida albicans fluoride channel FEX in complex with Fab fragment

Method: ELECTRON MICROSCOPY Dmax: 124.2 Å Quality: GOOD

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

Transmembrane protein gp41,Fluoride export protein 1

Candida albicans SC5314

UniProt P05877

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 670–686 Fragment:residues 76-389,residues 76-389 10E8v4 Fab Heavy Chian × 1 10E8v4 Fab Light Chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.05 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.

13 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENV_HV1MN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–19; UniProt 670–686

Transmembrane protein gp41,Fluoride export protein 1

Candida albicans SC5314

UniProt Q5AFH3

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 76–389 Fragment:residues 76-389,residues 76-389 10E8v4 Fab Heavy Chian × 1 10E8v4 Fab Light Chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.05 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name FEX1_CANAL
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 20–333; UniProt 76–389

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 9op1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9op1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9op1
Deposition date deposition_date2025-05-16
Structure title titleCryo-EM structure of Candida albicans fluoride channel FEX in complex with Fab fragment
Keywords keywordsFluoride channel, Fluoride exporter, FEX, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.73
Radius of gyration Rg (electron density) rg_electron36.15
Forward intensity I(0) i099551100.00
Molecular weight molecular_weight82750.0 kDa
Excluded volume excluded_volume104770 ų
Envelope volume envelope_volume142690 ų
Hydration-shell volume shell_volume35449 ų
Envelope diameter envelope_diameter132.5
Shell Rg shell_rg38.90
Envelope Rg envelope_rg36.21
Shape Rg shape_rg36.10
Total Rg total_rg36.51
Total atoms total_atoms5843
Residues n_residues745
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 dmax124.2
Rg (real space) rg_real36.11
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real9.9550e+07
I(0) uncertainty (real space) i0_real_error1.7470e+06
Rg (reciprocal space) rg_reciprocal35.87
I(0) (reciprocal space) i0_reciprocal99530000.0000
Solution quality estimate total_estimate0.8077
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.566
Kurtosis Kurtosis kurtosis-0.260
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16310000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.656; Smooth: 0.611

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)