7cn7

T4 phage spackle protein gp61.3 complex with lysozyme domain of gp5 tail lysozyme

Method: X-RAY DIFFRACTION Dmax: 60.6 Å Quality: GOOD

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

Baseplate central spike complex protein gp5

Enterobacteria phage T4

UniProt P16009

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 162–342 Not recorded Protein spackle × 1 (P39230) 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL × 1 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;PEG550MME, MES, KSCN Resolution 1.15 Å R-free 0.121

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.

17 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BP5_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–181; UniProt 162–342

Protein spackle

Enterobacteria phage T4

UniProt P39230

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 23–97 Not recorded Baseplate central spike complex protein gp5 × 1 (P16009) 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL × 1 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;PEG550MME, MES, KSCN Resolution 1.15 Å R-free 0.121

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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPAC_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–75; UniProt 23–97

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 7cn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7cn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7cn7
Deposition date deposition_date2020-07-30
Structure title titleT4 phage spackle protein gp61.3 complex with lysozyme domain of gp5 tail lysozyme
Keywords keywordsLysozyme inhibitor complex, Phage, Lysis inhibition, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.08
Radius of gyration Rg (electron density) rg_electron18.16
Forward intensity I(0) i015970800.00
Molecular weight molecular_weight29312.0 kDa
Excluded volume excluded_volume36401 ų
Envelope volume envelope_volume41576 ų
Hydration-shell volume shell_volume19015 ų
Envelope diameter envelope_diameter62.7
Shell Rg shell_rg24.49
Envelope Rg envelope_rg18.38
Shape Rg shape_rg18.15
Total Rg total_rg19.11
Total atoms total_atoms4075
Residues n_residues253
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 dmax60.6
Rg (real space) rg_real18.97
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.5970e+07
I(0) uncertainty (real space) i0_real_error1.9530e+05
Rg (reciprocal space) rg_reciprocal18.98
I(0) (reciprocal space) i0_reciprocal15970000.0000
Solution quality estimate total_estimate0.8975
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.0
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4584000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd7cn7a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id7cn7A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)