9sku

Cryo-EM structure of H. neapolitanus CsoSCA in reducing conditions, hexamer

Method: ELECTRON MICROSCOPY Dmax: 102.4 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Carboxysome shell carbonic anhydrase

Halothiobacillus neapolitanus c2

UniProt O85042

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 Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 2–514 Chain B; UniProt 2–514 Not recorded ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;4C, 100% relative humidity, delay time 0s, blot time 3s, blot force 0 Resolution 2.06 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.

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

View Construct and Data Evidence
UniProt name CSOCA_HALNC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 407–919; UniProt 2–514 Author chain B; PDBConstruct 407–919; UniProt 2–514

Maltose/maltodextrin-binding periplasmic protein,Carboxysome shell carbonic anhydrase

Halothiobacillus neapolitanus c2

UniProt P0AEX9

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 Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 27–392 Chain B; UniProt 27–392 Not recorded ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;4C, 100% relative humidity, delay time 0s, blot time 3s, blot force 0 Resolution 2.06 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–379; UniProt 27–392 Author chain B; PDBConstruct 14–379; UniProt 27–392

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 9sku

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9sku
Deposition date deposition_date2025-09-02
Structure title titleCryo-EM structure of H. neapolitanus CsoSCA in reducing conditions, hexamer
Keywords keywordsCarbonic anhydrase, carboxysome, CO2 concentration mechanism, LYASE; LYASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.76
Radius of gyration Rg (electron density) rg_electron32.17
Forward intensity I(0) i0176068000.00
Molecular weight molecular_weight104180.0 kDa
Excluded volume excluded_volume129600 ų
Envelope volume envelope_volume163460 ų
Hydration-shell volume shell_volume42689 ų
Envelope diameter envelope_diameter105.6
Shell Rg shell_rg38.92
Envelope Rg envelope_rg32.02
Shape Rg shape_rg32.17
Total Rg total_rg32.71
Total atoms total_atoms14370
Residues n_residues934
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 dmax102.4
Rg (real space) rg_real32.71
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.7610e+08
I(0) uncertainty (real space) i0_real_error2.3880e+06
Rg (reciprocal space) rg_reciprocal32.74
I(0) (reciprocal space) i0_reciprocal176100000.0000
Solution quality estimate total_estimate0.8971
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36850000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.830

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)