2xc1

Full-length Tailspike Protein Mutant Y108W of Bacteriophage P22

Method: X-RAY DIFFRACTION Dmax: 166.0 Å Quality: REASONABLE

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

BIFUNCTIONAL TAIL 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 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 2–667 Chain B; UniProt 2–667 Chain C; UniProt 2–667 Fragment:RESIDUES 2-667 Mutation:YES GOL GLYCEROL × 13 CA CALCIUM ION × 1 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 4 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;292 K;PROTEIN- 15MG/ML IN 10MM HEPES PH7;RESERVOIR:750 ML 0.2M AMMONIUM ACETATE,0.1M TRI-SODIUM CITRATE DIHYDRATE PH 5.6, 30% W/V POLYETHYLENE GLYCOL 4000; HANGING DROPS:1.5MICROL RESERVOIR- 1.5MICROL PROTEIN SOLUTION; TEMPERATURE: 19 DEGR.; CRYO: 3% GLYCEROL Resolution 1.65 Å R-free 0.210

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 1–666; UniProt 2–667 Author chain B; PDBConstruct 1–666; UniProt 2–667 Author chain C; PDBConstruct 1–666; UniProt 2–667

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 2xc1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xc1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2xc1
Deposition date deposition_date2010-04-15
Structure title titleFull-length Tailspike Protein Mutant Y108W of Bacteriophage P22
Keywords keywordsHYDROLASE, ENDOGLYCOSIDASE, SALMONELLA PHAGE P22; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.56
Radius of gyration Rg (electron density) rg_electron45.59
Forward intensity I(0) i0699185000.00
Molecular weight molecular_weight215710.0 kDa
Excluded volume excluded_volume269480 ų
Envelope volume envelope_volume340280 ų
Hydration-shell volume shell_volume67115 ų
Envelope diameter envelope_diameter174.5
Shell Rg shell_rg44.81
Envelope Rg envelope_rg46.54
Shape Rg shape_rg45.58
Total Rg total_rg45.57
Total atoms total_atoms15195
Residues n_residues1982
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 dmax166.0
Rg (real space) rg_real45.26
Rg uncertainty (real space) rg_real_error2.34
I(0) (real space) i0_real6.9920e+08
I(0) uncertainty (real space) i0_real_error1.3270e+07
Rg (reciprocal space) rg_reciprocal44.57
I(0) (reciprocal space) i0_reciprocal698600000.0000
Solution quality estimate total_estimate0.7473
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.7
Skewness Skewness skewness0.835
Kurtosis Kurtosis kurtosis0.573
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha129000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.505; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.647; Smooth: 0.549

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id2xc1A01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology14 — Tailspike Protein; Chain
Homologous superfamily homologous superfamily10 — Phage P22 tailspike-like, N-terminal domain
Domain ID domain_id2xc1A02
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily20
Domain ID domain_id2xc1B01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology14 — Tailspike Protein; Chain
Homologous superfamily homologous superfamily10 — Phage P22 tailspike-like, N-terminal domain
Domain ID domain_id2xc1B02
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily20
Domain ID domain_id2xc1C01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology14 — Tailspike Protein; Chain
Homologous superfamily homologous superfamily10 — Phage P22 tailspike-like, N-terminal domain
Domain ID domain_id2xc1C02
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)