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3o6a

F144Y/F258Y Double Mutant of Exo-beta-1,3-glucanase from Candida albicans at 2 A

Method: X-RAY DIFFRACTION Dmax: 64.3 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glucan 1,3-beta-glucosidase

Candida albicans

UniProt P29717

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 40–438 Mutation：F144Y, F258Y No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.3；291 K；0.1M HEPES-KOH, 0.2M CaCl2, 19% PEG 8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.00 Å R-free 0.200

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.

Other PDB Difference from Current Entry 3O6A Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CZ1 EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS AT 1.85 A RESOLUTION Deposited 1999-09-01 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 45–438（394 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；292 K；Hepes buffer, CaCl2, Peg 8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 1.85 Å R-free 0.196
1EQC EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS IN COMPLEX WITH CASTANOSPERMINE AT 1.85 A Deposited 2000-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 45–438（394 aa）
Not recorded CTS CASTANOSPERMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；291 K；HEPES BUFFER, CACL2, PEG8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.85 Å R-free 0.186
1EQP EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS Deposited 2000-04-05 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 45–438（394 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；291 K；HEPES BUFFER, CACL2, PEG 8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.90 Å R-free 0.195
3N9K F229A/E292S Double Mutant of Exo-beta-1,3-glucanase from Candida albicans in Complex with Laminaritriose at 1.7 A Deposited 2010-05-30 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 40–438（399 aa）
Mutation：F229A,E292S CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；291 K；0.1M HEPES-KOH, 0.2M CACL2, 19% PEG 8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.70 Å R-free 0.197

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXG_CANAL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–399； UniProt 40–438

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 3o6a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3o6a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3o6a
Deposition date deposition_date2010-07-28
Structure title titleF144Y/F258Y Double Mutant of Exo-beta-1,3-glucanase from Candida albicans at 2 A
Keywords keywordsTIM Barrel, Gycoside hydrolase family 5, Glycoside hydrolase, Secreted, Cell wall, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.62 Å
Radius of gyration Rg (electron density) rg_electron20.22 Å
Forward intensity I(0) i034580800.00
Molecular weight molecular_weight45247.0 kDa
Excluded volume excluded_volume56288 ų
Envelope volume envelope_volume64798 ų
Hydration-shell volume shell_volume25621 ų
Envelope diameter envelope_diameter67.7 Å
Shell Rg shell_rg27.84 Å
Envelope Rg envelope_rg20.45 Å
Shape Rg shape_rg20.19 Å
Total Rg total_rg21.23 Å
Total atoms total_atoms3216
Residues n_residues394
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax64.3 Å
Rg (real space) rg_real21.43 Å
Rg uncertainty (real space) rg_real_error0.24 Å
I(0) (real space) i0_real3.4580e+07
I(0) uncertainty (real space) i0_real_error4.4390e+05
Rg (reciprocal space) rg_reciprocal21.46 Å
I(0) (reciprocal space) i0_reciprocal34580000.0000
Solution quality estimate total_estimate0.9054
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4 Å
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.507
Angular range angular_range— – 0.3700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9091000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.981
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3o6aa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.8 — (Trans)glycosidases
Family Family familyc.1.8.3 — beta-glycanases

CATH v4.4 (1 domains)

Domain ID domain_id3o6aA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
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8. Citations (1)

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9. Files and Curves (10)