8uh7

Structure of T4 Bacteriophage clamp loader bound to the T4 clamp, primer-template DNA, and ATP analog

Method: X-RAY DIFFRACTION Dmax: 124.0 Å Quality: GOOD

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

Sliding-clamp-loader small subunit

Tequatrovirus

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–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–187 Not recorded Sliding-clamp-loader large subunit × 4 (P04526) Sliding clamp × 3 (P04525) Template DNA strand × 1 Primer DNA strand × 1 08T [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium × 3 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;295 K;20% PEG4k, 0.1M Tris pH7.5, 10mM MgCl2, 20mM NaCl Resolution 2.63 Å R-free 0.244

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–187; UniProt 1–187

Sliding-clamp-loader large subunit

Tequatrovirus

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–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts 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) Template DNA strand × 1 Primer DNA strand × 1 08T [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium × 3 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;295 K;20% PEG4k, 0.1M Tris pH7.5, 10mM MgCl2, 20mM NaCl Resolution 2.63 Å R-free 0.244

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 2
Chains and sequence ranges Author chain B; PDBConstruct 6–324; UniProt 1–319 Author chain C; PDBConstruct 6–324; UniProt 1–319 Author chain D; PDBConstruct 6–324; UniProt 1–319 Author chain E; PDBConstruct 6–324; UniProt 1–319

Sliding clamp

Tequatrovirus

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–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain F; UniProt 1–228 Chain G; UniProt 1–228 Chain H; UniProt 1–228 Non-standard monomer:Yes (specific site not provided by mmCIF) Sliding-clamp-loader small subunit × 1 (P04527) Sliding-clamp-loader large subunit × 4 (P04526) Template DNA strand × 1 Primer DNA strand × 1 08T [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium × 3 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;295 K;20% PEG4k, 0.1M Tris pH7.5, 10mM MgCl2, 20mM NaCl Resolution 2.63 Å R-free 0.244

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 8uh7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uh7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uh7
Deposition date deposition_date2023-10-07
Structure title titleStructure of T4 Bacteriophage clamp loader bound to the T4 clamp, primer-template DNA, and ATP analog
Keywords keywordsClamp loader, T4, AAA+ATPase, REPLICATION, REPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.95
Radius of gyration Rg (electron density) rg_electron40.77
Forward intensity I(0) i01966420000.00
Molecular weight molecular_weight237090.0 kDa
Excluded volume excluded_volume225620 ų
Envelope volume envelope_volume427310 ų
Hydration-shell volume shell_volume83534 ų
Envelope diameter envelope_diameter137.7
Shell Rg shell_rg49.13
Envelope Rg envelope_rg40.05
Shape Rg shape_rg40.82
Total Rg total_rg40.97
Total atoms total_atoms17766
Residues n_residues2168
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 dmax124.0
Rg (real space) rg_real40.78
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.9660e+09
I(0) uncertainty (real space) i0_real_error3.3270e+07
Rg (reciprocal space) rg_reciprocal40.95
I(0) (reciprocal space) i0_reciprocal1967000000.0000
Solution quality estimate total_estimate0.8273
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha163600000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)