6xc0

Crystal structure of bacteriophage T4 spackle and lysozyme in monoclinic form

Method: X-RAY DIFFRACTION Dmax: 90.2 Å Quality: GOOD

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

Lysozyme

Escherichia virus 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 174–342 Not recorded Protein spackle × 1 (P39230) EDO 1,2-ETHANEDIOL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SIN SUCCINIC ACID × 1 CL CHLORIDE ION × 1 FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;35% (w/v) polyethylene glycol 3350, 20% 2-propanol, 0.1 M HEPES-NaOH pH 7.5 Resolution 1.78 Å R-free 0.198
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 174–342 Not recorded Protein spackle × 1 (P39230) EDO 1,2-ETHANEDIOL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;35% (w/v) polyethylene glycol 3350, 20% 2-propanol, 0.1 M HEPES-NaOH pH 7.5 Resolution 1.78 Å R-free 0.198

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 24 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 1–169; UniProt 174–342 Author chain B; PDBConstruct 1–169; UniProt 174–342

Protein spackle

Escherichia virus 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 1–97 Not recorded Lysozyme × 1 (P16009) EDO 1,2-ETHANEDIOL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SIN SUCCINIC ACID × 1 CL CHLORIDE ION × 1 FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;35% (w/v) polyethylene glycol 3350, 20% 2-propanol, 0.1 M HEPES-NaOH pH 7.5 Resolution 1.78 Å R-free 0.198
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–97 Not recorded Lysozyme × 1 (P16009) EDO 1,2-ETHANEDIOL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;35% (w/v) polyethylene glycol 3350, 20% 2-propanol, 0.1 M HEPES-NaOH pH 7.5 Resolution 1.78 Å R-free 0.198

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 7 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 1–97; UniProt 1–97 Author chain D; PDBConstruct 1–97; UniProt 1–97

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 6xc0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xc0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6xc0
Deposition date deposition_date2020-06-07
Structure title titleCrystal structure of bacteriophage T4 spackle and lysozyme in monoclinic form
Keywords keywordslysozyme, spackle, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.81
Radius of gyration Rg (electron density) rg_electron26.27
Forward intensity I(0) i055140600.00
Molecular weight molecular_weight56188.0 kDa
Excluded volume excluded_volume69695 ų
Envelope volume envelope_volume84420 ų
Hydration-shell volume shell_volume27484 ų
Envelope diameter envelope_diameter95.4
Shell Rg shell_rg32.82
Envelope Rg envelope_rg26.13
Shape Rg shape_rg26.26
Total Rg total_rg26.99
Total atoms total_atoms3913
Residues n_residues485
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 dmax90.2
Rg (real space) rg_real26.87
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real5.5140e+07
I(0) uncertainty (real space) i0_real_error7.8710e+05
Rg (reciprocal space) rg_reciprocal26.85
I(0) (reciprocal space) i0_reciprocal55140000.0000
Solution quality estimate total_estimate0.8762
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.386
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19450000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.882; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6xc0a_
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
Domain ID domain_idd6xc0b_
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 (2 domains)

Domain ID domain_id6xc0A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40
Domain ID domain_id6xc0B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)