6drt

Crystal structure of the processivity clamp GP45 complexed with recognition peptide of ligase from bacteriophage T4

Method: X-RAY DIFFRACTION Dmax: 103.2 Å Quality: GOOD

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

DNA polymerase clamp

Enterobacteria phage 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–228 Chain B; UniProt 1–228 Chain C; UniProt 1–228 Not recorded GP45 recognition loop × 3 (P00970) EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;PEG3350 Resolution 2.12 Å R-free 0.240

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 DPA5_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–228; UniProt 1–228 Author chain B; PDBConstruct 1–228; UniProt 1–228 Author chain C; PDBConstruct 1–228; UniProt 1–228

GP45 recognition loop

OrganismNot specified

UniProt P00970

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 225–237 Chain E; UniProt 225–237 Chain F; UniProt 225–237 Not recorded DNA polymerase clamp × 3 (P04525) EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;PEG3350 Resolution 2.12 Å R-free 0.240

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNLI_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–13; UniProt 225–237 Author chain E; PDBConstruct 1–13; UniProt 225–237 Author chain F; PDBConstruct 1–13; UniProt 225–237

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 6drt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6drt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6drt
Deposition date deposition_date2018-06-13
Structure title titleCrystal structure of the processivity clamp GP45 complexed with recognition peptide of ligase from bacteriophage T4
Keywords keywordsHYDROLASE, processivity clamp, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.39
Radius of gyration Rg (electron density) rg_electron33.47
Forward intensity I(0) i093353100.00
Molecular weight molecular_weight78663.0 kDa
Excluded volume excluded_volume99251 ų
Envelope volume envelope_volume140750 ų
Hydration-shell volume shell_volume34368 ų
Envelope diameter envelope_diameter103.7
Shell Rg shell_rg41.44
Envelope Rg envelope_rg32.07
Shape Rg shape_rg33.51
Total Rg total_rg34.03
Total atoms total_atoms5541
Residues n_residues717
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 dmax103.2
Rg (real space) rg_real34.25
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real9.3350e+07
I(0) uncertainty (real space) i0_real_error1.5470e+06
Rg (reciprocal space) rg_reciprocal34.34
I(0) (reciprocal space) i0_reciprocal93360000.0000
Solution quality estimate total_estimate0.8921
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.8
Skewness Skewness skewness-0.016
Kurtosis Kurtosis kurtosis-0.856
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53110000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.925

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6drtA00
Class class3 — Alpha Beta
Architecture architecture70 — Box
Topology topology10 — Proliferating Cell Nuclear Antigen
Homologous superfamily homologous superfamily10
Domain ID domain_id6drtB00
Class class3 — Alpha Beta
Architecture architecture70 — Box
Topology topology10 — Proliferating Cell Nuclear Antigen
Homologous superfamily homologous superfamily10
Domain ID domain_id6drtC00
Class class3 — Alpha Beta
Architecture architecture70 — Box
Topology topology10 — Proliferating Cell Nuclear Antigen
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)