8ea4

V-K CAST Transpososome from Scytonema hofmanni, minor configuration

Method: ELECTRON MICROSCOPY Dmax: 230.2 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 × 24 DNA 6 RNA 1 PDB declaration: 31-meric(31) 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 Chain M; UniProt 1–276 Not recorded Cas12k × 1 (A0A8M0FGU0) TniQ × 1 (A0A8J0PCL5) 30S ribosomal protein S15 × 1 (D8EB41) TnsB × 8 Target-LE × 1 LE_R × 1 Non-target_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 sg_RNA × 1 MG MAGNESIUM ION × 15 ATP ADENOSINE-5'-TRIPHOSPHATE × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1
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 Author chain M; 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 × 24 DNA 6 RNA 1 PDB declaration: 31-meric(31) Consistent with all polymer counts Chain O; UniProt 1–639 Not recorded TnsC × 13 (A0A8J0PCL3) TniQ × 1 (A0A8J0PCL5) 30S ribosomal protein S15 × 1 (D8EB41) TnsB × 8 Target-LE × 1 LE_R × 1 Non-target_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 sg_RNA × 1 MG MAGNESIUM ION × 15 ATP ADENOSINE-5'-TRIPHOSPHATE × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 2
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 × 24 DNA 6 RNA 1 PDB declaration: 31-meric(31) Consistent with all polymer counts Chain Q; UniProt 1–167 Not recorded TnsC × 13 (A0A8J0PCL3) Cas12k × 1 (A0A8M0FGU0) 30S ribosomal protein S15 × 1 (D8EB41) TnsB × 8 Target-LE × 1 LE_R × 1 Non-target_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 sg_RNA × 1 MG MAGNESIUM ION × 15 ATP ADENOSINE-5'-TRIPHOSPHATE × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 3
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 × 24 DNA 6 RNA 1 PDB declaration: 31-meric(31) Consistent with all polymer counts Chain S; UniProt 1–89 Not recorded TnsC × 13 (A0A8J0PCL3) Cas12k × 1 (A0A8M0FGU0) TniQ × 1 (A0A8J0PCL5) TnsB × 8 Target-LE × 1 LE_R × 1 Non-target_R × 1 RE_F × 1 RE_R1 × 1 RE_R2 × 1 sg_RNA × 1 MG MAGNESIUM ION × 15 ATP ADENOSINE-5'-TRIPHOSPHATE × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 4
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 8ea4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ea4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ea4
Deposition date deposition_date2022-08-27
Structure title titleV-K CAST Transpososome from Scytonema hofmanni, minor configuration
Keywords keywordsDNA BINDING PROTEIN, DNA BINDING PROTEIN-RNA-DNA complex; DNA BINDING PROTEIN/RNA/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.40
Radius of gyration Rg (electron density) rg_electron78.57
Forward intensity I(0) i012665400000.00
Molecular weight molecular_weight835830.0 kDa
Excluded volume excluded_volume998920 ų
Envelope volume envelope_volume1643300 ų
Hydration-shell volume shell_volume184520 ų
Envelope diameter envelope_diameter305.6
Shell Rg shell_rg71.12
Envelope Rg envelope_rg78.06
Shape Rg shape_rg78.54
Total Rg total_rg78.57
Total atoms total_atoms58049
Residues n_residues6370
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 dmax230.2
Rg (real space) rg_real74.95
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.2180e+10
I(0) uncertainty (real space) i0_real_error2.1960e+08
Rg (reciprocal space) rg_reciprocal76.33
I(0) (reciprocal space) i0_reciprocal12560000000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary69.0
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.6006
Highest regularization parameter α highest_alpha1418000000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.912; Stabil: 0.976; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.086

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_id8ea4D01
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_id8ea4H01
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_id8ea4I01
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)