1qa1

TAILSPIKE PROTEIN, MUTANT V331G

Method: X-RAY DIFFRACTION Dmax: 127.7 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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 114–667 Fragment:RECEPTOR BINDING C-TERMINAL DOMAIN Mutation:V331G No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10;274 K;VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE Resolution 2.00 Å
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 114–667 Fragment:RECEPTOR BINDING C-TERMINAL DOMAIN Mutation:V331G No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10;274 K;VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE Resolution 2.00 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 32 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 1qa1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qa1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qa1
Deposition date deposition_date1999-04-10
Structure title titleTAILSPIKE PROTEIN, MUTANT V331G
Keywords keywordsvirus/viral protein, Viral protein-receptor COMPLEX; Viral protein/receptor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.57
Radius of gyration Rg (electron density) rg_electron33.60
Forward intensity I(0) i055344500.00
Molecular weight molecular_weight58249.0 kDa
Excluded volume excluded_volume72760 ų
Envelope volume envelope_volume97399 ų
Hydration-shell volume shell_volume27838 ų
Envelope diameter envelope_diameter135.1
Shell Rg shell_rg34.43
Envelope Rg envelope_rg34.92
Shape Rg shape_rg33.58
Total Rg total_rg33.73
Total atoms total_atoms5032
Residues n_residues542
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 dmax127.7
Rg (real space) rg_real33.40
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real5.5340e+07
I(0) uncertainty (real space) i0_real_error1.1220e+06
Rg (reciprocal space) rg_reciprocal33.04
I(0) (reciprocal space) i0_reciprocal55330000.0000
Solution quality estimate total_estimate0.6861
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.794
Kurtosis Kurtosis kurtosis0.114
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6994000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.295; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.197; Smooth: 0.832

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1qa1a_
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_id1qa1A00
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)