1tyx

TITLE OF TAILSPIKE-PROTEIN

Method: X-RAY DIFFRACTION Dmax: 128.3 Å Quality: REASONABLE

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

TAILSPIKE PROTEIN

Enterobacteria phage P22

UniProt P12528

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 3 其他Polymer 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 114–667 Fragment:RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN ;alpha-D-galactopyranose-(1-2)-[alpha-D-Abequopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose-(1-3)-alpha-D-galactopyranose-(1-2)-[alpha-D-Abequopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose ; × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;COMPLEX FORMED BY SOAKING WITH 2MM OCTASACCHARIDE FROM SALMONELLA TYPHIMURIUM O-ANTIGEN AT PH 7.5. Resolution 1.80 Å

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.

28 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TSPE_BPP22
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–554; UniProt 114–667

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 1tyx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tyx
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1tyx
Deposition date deposition_date1996-07-26
Structure title titleTITLE OF TAILSPIKE-PROTEIN
Keywords keywords;COMPLEX, VIRAL ADHESION PROTEIN, RECEPTOR, ENDOGLYCOSIDASE CARBOHYDRATE, CELL RECEPTOR, RECOGNITION, BINDING PROTEIN LIPOPOLYSACCHARIDE ;; VIRAL ADHESION PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.37
Radius of gyration Rg (electron density) rg_electron33.35
Forward intensity I(0) i057630900.00
Molecular weight molecular_weight59604.0 kDa
Excluded volume excluded_volume74503 ų
Envelope volume envelope_volume99544 ų
Hydration-shell volume shell_volume28420 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg34.45
Envelope Rg envelope_rg34.97
Shape Rg shape_rg33.34
Total Rg total_rg33.47
Total atoms total_atoms4198
Residues n_residues543
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 dmax128.3
Rg (real space) rg_real33.20
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real5.7630e+07
I(0) uncertainty (real space) i0_real_error1.1110e+06
Rg (reciprocal space) rg_reciprocal32.84
I(0) (reciprocal space) i0_reciprocal57610000.0000
Solution quality estimate total_estimate0.6815
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.807
Kurtosis Kurtosis kurtosis0.133
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9229000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.248; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.162; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tyxa_
Class classb — All beta proteins
Fold Fold foldb.80 — Single-stranded right-handed beta-helix
Superfamily Superfamily superfamilyb.80.1 — Pectin lyase-like
Family Family familyb.80.1.6 — P22 tailspike protein

CATH v4.4 (1 domains)

Domain ID domain_id1tyxA00
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily20

8. Citations (3)

9. Files and Curves (10)