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9xvg

Maltoheptaose-incubated Arabidopsis ISA1-ISA1 homodimer

Method: ELECTRON MICROSCOPY Dmax: 172.6 Å Quality: SUSPICIOUS
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Isoamylase 1, chloroplastic

Arabidopsis thaliana

UniProt O04196

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 44–783 Chain B； UniProt 44–783 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.49 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 9XVG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9XVE Arabidopsis ISA1-ISA1 homodimer Deposited 2025-11-26 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 44–783（740 aa）
Chain B 44–783（740 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.36 Å
9XVI Arabidopsis ISA2-ISA1-ISA1-ISA2 heterotetramer Deposited 2025-11-26 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 44–783（740 aa）
Chain B 44–783（740 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.65 Å
9XVP Arabidopsis ISA2-ISA1-ISA1 heterotrimer Deposited 2025-11-26 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–783（740 aa）
Chain B 44–783（740 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.38 Å
9XVV Maltoheptaose-bound Arabidopsis ISA2-ISA1-ISA1 heterotrimer Deposited 2025-11-27 Different oligomeric state Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–783（740 aa）
Chain B 44–783（740 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.49 Å

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

View Construct and Data Evidence
UniProt name ISOA1_ARATH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 42–781； UniProt 44–783 Author chain B； PDBConstruct 42–781； UniProt 44–783

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 9xvg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xvg
Deposition date deposition_date2025-11-26
Structure title titleMaltoheptaose-incubated Arabidopsis ISA1-ISA1 homodimer
Keywords keywordsisoamylase, ISA1, ISA2, PLANT PROTEIN; PLANT 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_guinier49.49 Å
Radius of gyration Rg (electron density) rg_electron50.72 Å
Forward intensity I(0) i0333522000.00
Molecular weight molecular_weight149040.0 kDa
Excluded volume excluded_volume185490 ų
Envelope volume envelope_volume255440 ų
Hydration-shell volume shell_volume47754 ų
Envelope diameter envelope_diameter186.3 Å
Shell Rg shell_rg44.78 Å
Envelope Rg envelope_rg51.38 Å
Shape Rg shape_rg50.74 Å
Total Rg total_rg50.42 Å
Total atoms total_atoms10512
Residues n_residues1295
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 dmax172.6 Å
Rg (real space) rg_real51.92 Å
Rg uncertainty (real space) rg_real_error0.86 Å
I(0) (real space) i0_real3.3400e+08
I(0) uncertainty (real space) i0_real_error5.8170e+06
Rg (reciprocal space) rg_reciprocal49.51 Å
I(0) (reciprocal space) i0_reciprocal332900000.0000
Solution quality estimate total_estimate0.4836
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.4 Å
Skewness Skewness skewness0.631
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.1600 Å−1
Current regularization parameter α current_alpha1.4130
Highest regularization parameter α highest_alpha74050000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.352; Stabil: 0.948; Sysdev: 0.000; Positv: 1.000; Valcen: 0.247; Smooth: 0.140
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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)