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9x2b

Cryo-EM structure of PsoA in apo state (PsoA-PKS-II)

Method: ELECTRON MICROSCOPY Dmax: 206.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PKS-NRPS hybrid synthetase psoA

Aspergillus fumigatus Af293

UniProt Q4WAZ9

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–4007 Chain B； UniProt 1–4007 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.39 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.

Other PDB Difference from Current Entry 9X2B Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9X29 Cryo-EM structure of PsoA in cofactor bound state (PsoA-PKS-I) Deposited 2025-10-04 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–4007（4007 aa）
Chain B 1–4007（4007 aa）
Not recorded MLC MALONYL-COENZYME A × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.16 Å
9X2A Cryo-EM structure of PsoA in cofactor bound state (PsoA-PKS-II) Deposited 2025-10-04 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–4007（4007 aa）
Chain B 1–4007（4007 aa）
Not recorded COZ COENZYME A × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.36 Å
9X2C Cryo-EM structure of PsoA in apo state (PsoA-PKS-I) Deposited 2025-10-04 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–4007（4007 aa）
Chain B 1–4007（4007 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.99 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSOA_ASPFU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–4007； UniProt 1–4007 Author chain B； PDBConstruct 1–4007； UniProt 1–4007

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 9x2b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x2b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x2b
Deposition date deposition_date2025-10-04
Structure title titleCryo-EM structure of PsoA in apo state (PsoA-PKS-II)
Keywords keywordsPKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of pseurotin A, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier68.94 Å
Radius of gyration Rg (electron density) rg_electron69.25 Å
Forward intensity I(0) i03805040000.00
Molecular weight molecular_weight515230.0 kDa
Excluded volume excluded_volume642850 ų
Envelope volume envelope_volume1023200 ų
Hydration-shell volume shell_volume127210 ų
Envelope diameter envelope_diameter223.8 Å
Shell Rg shell_rg64.91 Å
Envelope Rg envelope_rg67.05 Å
Shape Rg shape_rg69.23 Å
Total Rg total_rg69.25 Å
Total atoms total_atoms72161
Residues n_residues4733
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 dmax206.7 Å
Rg (real space) rg_real68.90 Å
Rg uncertainty (real space) rg_real_error1.67 Å
I(0) (real space) i0_real3.8050e+09
I(0) uncertainty (real space) i0_real_error7.7840e+07
Rg (reciprocal space) rg_reciprocal68.91 Å
I(0) (reciprocal space) i0_reciprocal3805000000.0000
Solution quality estimate total_estimate0.8387
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary98.9 Å
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.1150 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha207400000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.055
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)