9zs2

S. marcescens Cas10-Csm unbound to target RNA

Method: ELECTRON MICROSCOPY Dmax: 192.7 Å Quality: REASONABLE

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

CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A)

Serratia

UniProt A0A2I5TNR6

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–RNA Heteromer Protein × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 1–816 Not recorded CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) RNA (30-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2I5TNR6_SERS3
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–816; UniProt 1–816

CRISPR system Cms endoribonuclease Csm3

Serratia

UniProt A0A2I5TNQ0

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–RNA Heteromer Protein × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain E; UniProt 1–248 Chain F; UniProt 1–248 Chain G; UniProt 1–248 Chain H; UniProt 1–248 Mutation:D43A CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) × 1 (A0A2I5TNR6) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) RNA (30-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2I5TNQ0_SERS3
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–248; UniProt 1–248 Author chain F; PDBConstruct 1–248; UniProt 1–248 Author chain G; PDBConstruct 1–248; UniProt 1–248 Author chain H; PDBConstruct 1–248; UniProt 1–248

CRISPR system Cms protein Csm4

Serratia

UniProt A0A2I5TQV2

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–RNA Heteromer Protein × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain I; UniProt 1–326 Not recorded CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) × 1 (A0A2I5TNR6) CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) RNA (30-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2I5TQV2_SERS3
Isoform
PDB entities 3
Chains and sequence ranges Author chain I; PDBConstruct 1–326; UniProt 1–326

CRISPR system Cms protein Csm5

Serratia

UniProt A0A2I5TBB3

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–RNA Heteromer Protein × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain J; UniProt 1–559 Not recorded CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) × 1 (A0A2I5TNR6) CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) RNA (30-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2I5TBB3_SERS3
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 1–559; UniProt 1–559

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 9zs2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zs2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9zs2
Deposition date deposition_date2025-12-22
Structure title titleS. marcescens Cas10-Csm unbound to target RNA
Keywords keywordsCRISPR, crRNA, Cas10, type III, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.33
Radius of gyration Rg (electron density) rg_electron59.48
Forward intensity I(0) i01059700000.00
Molecular weight molecular_weight263530.0 kDa
Excluded volume excluded_volume326300 ų
Envelope volume envelope_volume482400 ų
Hydration-shell volume shell_volume70416 ų
Envelope diameter envelope_diameter215.3
Shell Rg shell_rg56.08
Envelope Rg envelope_rg59.61
Shape Rg shape_rg59.49
Total Rg total_rg59.37
Total atoms total_atoms18542
Residues n_residues2338
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 dmax192.7
Rg (real space) rg_real59.08
Rg uncertainty (real space) rg_real_error2.22
I(0) (real space) i0_real1.0600e+09
I(0) uncertainty (real space) i0_real_error2.3950e+07
Rg (reciprocal space) rg_reciprocal57.65
I(0) (reciprocal space) i0_reciprocal1057000000.0000
Solution quality estimate total_estimate0.7386
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.8
Skewness Skewness skewness0.531
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118700000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.584; Smooth: 0.057

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)