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9xvv

Maltoheptaose-bound Arabidopsis ISA2-ISA1-ISA1 heterotrimer

Method: ELECTRON MICROSCOPY Dmax: 207.2 Å Quality: REASONABLE
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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 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 44–783 Chain B； UniProt 44–783 Not recorded Isoamylase 2, chloroplastic × 1 （Q8L735） ;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose ; × 1 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 9XVV 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 oligomeric state 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
9XVG Maltoheptaose-incubated Arabidopsis ISA1-ISA1 homodimer Deposited 2025-11-26 Different oligomeric state 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 2.49 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

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 25–764； UniProt 44–783 Author chain B； PDBConstruct 25–764； UniProt 44–783

Isoamylase 2, chloroplastic

Arabidopsis thaliana

UniProt Q8L735

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 Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric（3） Consistent with protein copy count Chain C； UniProt 54–882 Not recorded Isoamylase 1, chloroplastic × 2 （O04196） ;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose ; × 1 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 9XVV Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9XVI Arabidopsis ISA2-ISA1-ISA1-ISA2 heterotetramer Deposited 2025-11-26 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 54–882（829 aa）
Chain D 54–882（829 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 C 54–882（829 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

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ISOA2_ARATH
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 42–870； UniProt 54–882

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 9xvv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xvv
Deposition date deposition_date2025-11-27
Structure title titleMaltoheptaose-bound Arabidopsis ISA2-ISA1-ISA1 heterotrimer
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_guinier56.77 Å
Radius of gyration Rg (electron density) rg_electron57.94 Å
Forward intensity I(0) i0822165000.00
Molecular weight molecular_weight237660.0 kDa
Excluded volume excluded_volume296580 ų
Envelope volume envelope_volume424020 ų
Hydration-shell volume shell_volume69170 ų
Envelope diameter envelope_diameter226.5 Å
Shell Rg shell_rg50.08 Å
Envelope Rg envelope_rg58.31 Å
Shape Rg shape_rg57.93 Å
Total Rg total_rg57.73 Å
Total atoms total_atoms16763
Residues n_residues2076
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 dmax207.2 Å
Rg (real space) rg_real57.81 Å
Rg uncertainty (real space) rg_real_error2.49 Å
I(0) (real space) i0_real8.2210e+08
I(0) uncertainty (real space) i0_real_error1.7360e+07
Rg (reciprocal space) rg_reciprocal55.90 Å
I(0) (reciprocal space) i0_reciprocal819800000.0000
Solution quality estimate total_estimate0.7085
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.4 Å
Skewness Skewness skewness0.729
Kurtosis Kurtosis kurtosis-0.080
Angular range angular_range— – 0.1400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84410000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.429; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.437; Smooth: 0.483
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)