7sj5

Bacteriophage lambda major capsid protein mutant - W308A

Method: X-RAY DIFFRACTION Dmax: 119.2 Å Quality: REASONABLE

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

Major capsid protein

Escherichia phage lambda

UniProt P03713

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–341 Chain B; UniProt 1–341 Chain C; UniProt 1–341 Chain D; UniProt 1–341 Mutation:W308A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;291.15 K;0.1 M bis-tris, 0.1 M ammonium sulfate, 5% v/v glycerol, 30% v/v PEG-3350 Resolution 2.69 Å R-free 0.230

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.

7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPSD_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–341; UniProt 1–341 Author chain B; PDBConstruct 1–341; UniProt 1–341 Author chain C; PDBConstruct 1–341; UniProt 1–341 Author chain D; PDBConstruct 1–341; UniProt 1–341

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 7sj5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7sj5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7sj5
Deposition date deposition_date2021-10-15
Structure title titleBacteriophage lambda major capsid protein mutant - W308A
Keywords keywordsmajor capsid protein, HK97-fold, assembly incompetent, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.90
Radius of gyration Rg (electron density) rg_electron36.00
Forward intensity I(0) i0356279000.00
Molecular weight molecular_weight151290.0 kDa
Excluded volume excluded_volume188780 ų
Envelope volume envelope_volume256830 ų
Hydration-shell volume shell_volume58000 ų
Envelope diameter envelope_diameter128.5
Shell Rg shell_rg43.75
Envelope Rg envelope_rg35.41
Shape Rg shape_rg35.99
Total Rg total_rg36.54
Total atoms total_atoms10638
Residues n_residues1360
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 dmax119.2
Rg (real space) rg_real36.72
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real3.5630e+08
I(0) uncertainty (real space) i0_real_error5.2970e+06
Rg (reciprocal space) rg_reciprocal36.83
I(0) (reciprocal space) i0_reciprocal356300000.0000
Solution quality estimate total_estimate0.6770
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.1
Skewness Skewness skewness0.167
Kurtosis Kurtosis kurtosis-0.464
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63560000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 0.048; Positv: 1.000; Valcen: 0.998; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7sj5A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1930 — capsid protein of prophage fold
Homologous superfamily homologous superfamily10 — capsid protein of prophage domain
Domain ID domain_id7sj5B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1930 — capsid protein of prophage fold
Homologous superfamily homologous superfamily10 — capsid protein of prophage domain
Domain ID domain_id7sj5C01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1930 — capsid protein of prophage fold
Homologous superfamily homologous superfamily10 — capsid protein of prophage domain
Domain ID domain_id7sj5D01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1930 — capsid protein of prophage fold
Homologous superfamily homologous superfamily10 — capsid protein of prophage domain

8. Citations (1)

9. Files and Curves (10)