8ea3

V-K CAST Transpososome from Scytonema hofmanni, major configuration

Method: ELECTRON MICROSCOPY Dmax: 226.7 Å Quality: EXCELLENT

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

TnsC

Scytonema hofmannii

UniProt A0A8J0PCL3

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 × 23 DNA 6 RNA 1 PDB declaration: 30-meric(30) Consistent with all polymer counts Chain A; UniProt 1–276 Chain B; UniProt 1–276 Chain C; UniProt 1–276 Chain D; UniProt 1–276 Chain E; UniProt 1–276 Chain F; UniProt 1–276 Chain G; UniProt 1–276 Chain H; UniProt 1–276 Chain I; UniProt 1–276 Chain J; UniProt 1–276 Chain K; UniProt 1–276 Chain L; UniProt 1–276 Not recorded Target_LE × 1 Non-target_R × 1 sg_RNA × 1 Cas12k × 1 (A0A8M0FGU0) TniQ × 1 (A0A8J0PCL5) 30S ribosomal protein S15 × 1 (D8EB41) TnsB × 8 LE_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0PCL3_9CYAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 1–276 Author chain B; PDBConstruct 1–276; UniProt 1–276 Author chain C; PDBConstruct 1–276; UniProt 1–276 Author chain D; PDBConstruct 1–276; UniProt 1–276 Author chain E; PDBConstruct 1–276; UniProt 1–276 Author chain F; PDBConstruct 1–276; UniProt 1–276 Author chain G; PDBConstruct 1–276; UniProt 1–276 Author chain H; PDBConstruct 1–276; UniProt 1–276 Author chain I; PDBConstruct 1–276; UniProt 1–276 Author chain J; PDBConstruct 1–276; UniProt 1–276 Author chain K; PDBConstruct 1–276; UniProt 1–276 Author chain L; PDBConstruct 1–276; UniProt 1–276

Cas12k

Scytonema hofmannii

UniProt A0A8M0FGU0

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 × 23 DNA 6 RNA 1 PDB declaration: 30-meric(30) Consistent with all polymer counts Chain O; UniProt 1–639 Not recorded Target_LE × 1 Non-target_R × 1 sg_RNA × 1 TnsC × 12 (A0A8J0PCL3) TniQ × 1 (A0A8J0PCL5) 30S ribosomal protein S15 × 1 (D8EB41) TnsB × 8 LE_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8M0FGU0_9CYAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain O; PDBConstruct 1–639; UniProt 1–639

TniQ

Scytonema hofmannii

UniProt A0A8J0PCL5

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 × 23 DNA 6 RNA 1 PDB declaration: 30-meric(30) Consistent with all polymer counts Chain Q; UniProt 1–167 Not recorded Target_LE × 1 Non-target_R × 1 sg_RNA × 1 TnsC × 12 (A0A8J0PCL3) Cas12k × 1 (A0A8M0FGU0) 30S ribosomal protein S15 × 1 (D8EB41) TnsB × 8 LE_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0PCL5_9CYAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain Q; PDBConstruct 1–167; UniProt 1–167

30S ribosomal protein S15

Escherichia coli

UniProt D8EB41

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 × 23 DNA 6 RNA 1 PDB declaration: 30-meric(30) Consistent with all polymer counts Chain S; UniProt 1–89 Not recorded Target_LE × 1 Non-target_R × 1 sg_RNA × 1 TnsC × 12 (A0A8J0PCL3) Cas12k × 1 (A0A8M0FGU0) TniQ × 1 (A0A8J0PCL5) TnsB × 8 LE_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D8EB41_ECOLX
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–89; UniProt 1–89

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 8ea3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ea3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ea3
Deposition date deposition_date2022-08-27
Structure title titleV-K CAST Transpososome from Scytonema hofmanni, major configuration
Keywords keywordsDNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA-RNA complex; DNA BINDING PROTEIN/DNA/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier78.86
Radius of gyration Rg (electron density) rg_electron77.99
Forward intensity I(0) i011894300000.00
Molecular weight molecular_weight805970.0 kDa
Excluded volume excluded_volume961420 ų
Envelope volume envelope_volume1608400 ų
Hydration-shell volume shell_volume180870 ų
Envelope diameter envelope_diameter305.6
Shell Rg shell_rg70.53
Envelope Rg envelope_rg78.06
Shape Rg shape_rg77.95
Total Rg total_rg77.99
Total atoms total_atoms55955
Residues n_residues6113
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 dmax226.7
Rg (real space) rg_real74.53
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real1.1440e+10
I(0) uncertainty (real space) i0_real_error2.0680e+08
Rg (reciprocal space) rg_reciprocal75.91
I(0) (reciprocal space) i0_reciprocal11800000000.0000
Solution quality estimate total_estimate0.9069
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.0
Skewness Skewness skewness0.506
Kurtosis Kurtosis kurtosis-0.358
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.6180
Highest regularization parameter α highest_alpha1255000000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.927; Stabil: 0.981; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.073

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8ea3D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id8ea3G01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id8ea3H01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)