9zs4

S. marcescens Cas10-Csm bound to target RNA

Method: ELECTRON MICROSCOPY Dmax: 194.1 Å Quality: GOOD

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 × 10 RNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain A; UniProt 1–816 Not recorded crRNA × 1 Target RNA × 1 CRISPR system Cms protein Csm2 × 3 (A0A2I5TBC8) CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 protein Csm2

Serratia

UniProt A0A2I5TBC8

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 × 10 RNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain B; UniProt 2–127 Chain C; UniProt 2–127 Chain D; UniProt 2–127 Not recorded CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) × 1 (A0A2I5TNR6) crRNA × 1 Target RNA × 1 CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A2I5TBC8_SERS3
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 8–133; UniProt 2–127 Author chain C; PDBConstruct 8–133; UniProt 2–127 Author chain D; PDBConstruct 8–133; UniProt 2–127

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 × 10 RNA 2 PDB declaration: 12-meric(12) 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:D34A CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) × 1 (A0A2I5TNR6) crRNA × 1 Target RNA × 1 CRISPR system Cms protein Csm2 × 3 (A0A2I5TBC8) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 5
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 × 10 RNA 2 PDB declaration: 12-meric(12) 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) crRNA × 1 Target RNA × 1 CRISPR system Cms protein Csm2 × 3 (A0A2I5TBC8) CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm5 × 1 (A0A2I5TBB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 6
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 × 10 RNA 2 PDB declaration: 12-meric(12) 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) crRNA × 1 Target RNA × 1 CRISPR system Cms protein Csm2 × 3 (A0A2I5TBC8) CRISPR system Cms endoribonuclease Csm3 × 4 (A0A2I5TNQ0) CRISPR system Cms protein Csm4 × 1 (A0A2I5TQV2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 7
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 9zs4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zs4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zs4
Deposition date deposition_date2025-12-22
Structure title titleS. marcescens Cas10-Csm bound 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_guinier56.03
Radius of gyration Rg (electron density) rg_electron57.10
Forward intensity I(0) i01828300000.00
Molecular weight molecular_weight340340.0 kDa
Excluded volume excluded_volume419080 ų
Envelope volume envelope_volume614790 ų
Hydration-shell volume shell_volume92902 ų
Envelope diameter envelope_diameter205.9
Shell Rg shell_rg54.95
Envelope Rg envelope_rg57.46
Shape Rg shape_rg57.11
Total Rg total_rg57.02
Total atoms total_atoms23910
Residues n_residues2930
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 dmax194.1
Rg (real space) rg_real56.57
Rg uncertainty (real space) rg_real_error2.19
I(0) (real space) i0_real1.8280e+09
I(0) uncertainty (real space) i0_real_error3.6390e+07
Rg (reciprocal space) rg_reciprocal55.57
I(0) (reciprocal space) i0_reciprocal1826000000.0000
Solution quality estimate total_estimate0.7883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.5
Skewness Skewness skewness0.588
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha545900000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.677; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.861; Smooth: 0.353

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)