8unh

Cryo-EM structure of T4 Bacteriophage Clamp Loader with Sliding Clamp

Method: ELECTRON MICROSCOPY Dmax: 122.5 Å Quality: GOOD

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

Sliding-clamp-loader large subunit

Tequatrovirus T4

UniProt P04526

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–319 Chain C; UniProt 1–319 Chain D; UniProt 1–319 Chain E; UniProt 1–319 Not recorded Sliding-clamp-loader small subunit × 1 (P04527) Sliding clamp × 3 (P04525) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOADL_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–319; UniProt 1–319 Author chain C; PDBConstruct 1–319; UniProt 1–319 Author chain D; PDBConstruct 1–319; UniProt 1–319 Author chain E; PDBConstruct 1–319; UniProt 1–319

Sliding-clamp-loader small subunit

Tequatrovirus T4

UniProt P04527

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–187 Not recorded Sliding-clamp-loader large subunit × 4 (P04526) Sliding clamp × 3 (P04525) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOADS_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–187; UniProt 1–187

Sliding clamp

Tequatrovirus T4

UniProt P04525

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–228 Chain G; UniProt 1–228 Chain H; UniProt 1–228 Not recorded Sliding-clamp-loader large subunit × 4 (P04526) Sliding-clamp-loader small subunit × 1 (P04527) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLAMP_BPT4
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–228; UniProt 1–228 Author chain G; PDBConstruct 1–228; UniProt 1–228 Author chain H; PDBConstruct 1–228; UniProt 1–228

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 8unh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8unh
Deposition date deposition_date2023-10-19
Structure title titleCryo-EM structure of T4 Bacteriophage Clamp Loader with Sliding Clamp
Keywords keywordsautoinhibited, DNA-free, catalytically inactive, stable, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.43
Radius of gyration Rg (electron density) rg_electron39.84
Forward intensity I(0) i0518549000.00
Molecular weight molecular_weight188530.0 kDa
Excluded volume excluded_volume237100 ų
Envelope volume envelope_volume328160 ų
Hydration-shell volume shell_volume67435 ų
Envelope diameter envelope_diameter128.2
Shell Rg shell_rg47.46
Envelope Rg envelope_rg37.98
Shape Rg shape_rg39.82
Total Rg total_rg40.34
Total atoms total_atoms13271
Residues n_residues1683
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 dmax122.5
Rg (real space) rg_real40.19
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real5.1860e+08
I(0) uncertainty (real space) i0_real_error8.3450e+06
Rg (reciprocal space) rg_reciprocal40.43
I(0) (reciprocal space) i0_reciprocal518700000.0000
Solution quality estimate total_estimate0.8970
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.5
Skewness Skewness skewness-0.013
Kurtosis Kurtosis kurtosis-0.549
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38210000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.917

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)