1wth

Crystal structure of gp5-S351L mutant and gp27 complex

Method: X-RAY DIFFRACTION Dmax: 189.3 Å Quality: REASONABLE

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

Tail-associated lysozyme

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–575 Mutation:S351L Baseplate structural protein Gp27 × 3 (P17172) K POTASSIUM ION × 3 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;279 K;PEG 8000, Tris, Glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 2.80 Å R-free 0.281

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 VG05_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–575; UniProt 1–575

Baseplate structural protein Gp27

Enterobacteria phage T4

UniProt P17172

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 1–391 Not recorded Tail-associated lysozyme × 3 (P16009) K POTASSIUM ION × 3 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;279 K;PEG 8000, Tris, Glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 2.80 Å R-free 0.281

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VG27_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–391; UniProt 1–391

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 1wth

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1wth
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1wth
Deposition date deposition_date2004-11-23
Structure title titleCrystal structure of gp5-S351L mutant and gp27 complex
Keywords keywordsTriple-stranded beta-helix, OB fold, pseudohexamer, T4 tail lysozyme, HUB, gp5-gp27, Hydrolase-Structural protein COMPLEX; Hydrolase/Structural protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.73
Radius of gyration Rg (electron density) rg_electron50.34
Forward intensity I(0) i0167562000.00
Molecular weight molecular_weight103860.0 kDa
Excluded volume excluded_volume129160 ų
Envelope volume envelope_volume217350 ų
Hydration-shell volume shell_volume39677 ų
Envelope diameter envelope_diameter201.2
Shell Rg shell_rg45.22
Envelope Rg envelope_rg53.55
Shape Rg shape_rg50.31
Total Rg total_rg50.19
Total atoms total_atoms7297
Residues n_residues932
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 dmax189.3
Rg (real space) rg_real50.09
Rg uncertainty (real space) rg_real_error3.81
I(0) (real space) i0_real1.6760e+08
I(0) uncertainty (real space) i0_real_error3.5530e+06
Rg (reciprocal space) rg_reciprocal48.74
I(0) (reciprocal space) i0_reciprocal167300000.0000
Solution quality estimate total_estimate0.6606
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.717
Kurtosis Kurtosis kurtosis-0.031
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11650000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.264; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.119; Smooth: 0.674

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1wthd1
Class classb — All beta proteins
Fold Fold foldb.106 — Phage tail proteins
Superfamily Superfamily superfamilyb.106.1 — Phage tail proteins
Family Family familyb.106.1.1 — Baseplate protein-like
Domain ID domain_idd1wthd2
Class classb — All beta proteins
Fold Fold foldb.106 — Phage tail proteins
Superfamily Superfamily superfamilyb.106.1 — Phage tail proteins
Family Family familyb.106.1.1 — Baseplate protein-like

CATH v4.4 (7 domains)

Domain ID domain_id1wthA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily260 — Nucleic acid-binding protein domain
Domain ID domain_id1wthA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily190
Domain ID domain_id1wthA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40
Domain ID domain_id1wthD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1wthD02
Class class3 — Alpha Beta
Architecture architecture55 — 3-Layer(bab) Sandwich
Topology topology50 — Phage tail protein beta-alpha-beta fold
Homologous superfamily homologous superfamily20
Domain ID domain_id1wthD03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily150 — Bacteriophage T4, Gp27, baseplate hub, domain 3
Domain ID domain_id1wthD04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1920 — Phage tail proteins - 2 layer sandwich fold
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)