9xqd

The structure of outer peripheral region in the phage phiKZ baseplate complex

Method: ELECTRON MICROSCOPY Dmax: 262.3 Å Quality: EXCELLENT

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

PHIKZ026

OrganismNot specified

UniProt Q8SDD6

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 × 23 PDB declaration: 23-meric(23) Consistent with protein copy count Chain a; UniProt 1–552 Chain b; UniProt 1–552 Chain c; UniProt 1–552 Chain d; UniProt 1–552 Chain e; UniProt 1–552 Chain f; UniProt 1–552 Not recorded PHIKZ027 × 2 (Q8SDD5) PHIKZ127 × 1 (Q8SD35) PHIKZ130 × 2 (Q8SD32) PHIKZ139 × 6 (Q8SD23) PHIKZ157 × 6 (Q8SD05) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.53 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8SDD6_BPDPK
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–552; UniProt 1–552 Author chain b; PDBConstruct 1–552; UniProt 1–552 Author chain c; PDBConstruct 1–552; UniProt 1–552 Author chain d; PDBConstruct 1–552; UniProt 1–552 Author chain e; PDBConstruct 1–552; UniProt 1–552 Author chain f; PDBConstruct 1–552; UniProt 1–552

PHIKZ027

OrganismNot specified

UniProt Q8SDD5

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 × 23 PDB declaration: 23-meric(23) Consistent with protein copy count Chain G; UniProt 1–898 Chain K; UniProt 1–898 Not recorded PHIKZ026 × 6 (Q8SDD6) PHIKZ127 × 1 (Q8SD35) PHIKZ130 × 2 (Q8SD32) PHIKZ139 × 6 (Q8SD23) PHIKZ157 × 6 (Q8SD05) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.53 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8SDD5_BPDPK
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–898; UniProt 1–898 Author chain K; PDBConstruct 1–898; UniProt 1–898

PHIKZ127

OrganismNot specified

UniProt Q8SD35

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 × 23 PDB declaration: 23-meric(23) Consistent with protein copy count Chain 0; UniProt 1–290 Not recorded PHIKZ026 × 6 (Q8SDD6) PHIKZ027 × 2 (Q8SDD5) PHIKZ130 × 2 (Q8SD32) PHIKZ139 × 6 (Q8SD23) PHIKZ157 × 6 (Q8SD05) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.53 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8SD35_BPDPK
Isoform
PDB entities 3
Chains and sequence ranges Author chain 0; PDBConstruct 1–290; UniProt 1–290

PHIKZ130

OrganismNot specified

UniProt Q8SD32

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 × 23 PDB declaration: 23-meric(23) Consistent with protein copy count Chain H; UniProt 1–427 Chain L; UniProt 1–427 Not recorded PHIKZ026 × 6 (Q8SDD6) PHIKZ027 × 2 (Q8SDD5) PHIKZ127 × 1 (Q8SD35) PHIKZ139 × 6 (Q8SD23) PHIKZ157 × 6 (Q8SD05) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.53 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8SD32_BPDPK
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–427; UniProt 1–427 Author chain L; PDBConstruct 1–427; UniProt 1–427

PHIKZ139

OrganismNot specified

UniProt Q8SD23

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 × 23 PDB declaration: 23-meric(23) Consistent with protein copy count Chain 1; UniProt 1–298 Chain 2; UniProt 1–298 Chain 3; UniProt 1–298 Chain 4; UniProt 1–298 Chain 5; UniProt 1–298 Chain 6; UniProt 1–298 Not recorded PHIKZ026 × 6 (Q8SDD6) PHIKZ027 × 2 (Q8SDD5) PHIKZ127 × 1 (Q8SD35) PHIKZ130 × 2 (Q8SD32) PHIKZ157 × 6 (Q8SD05) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.53 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8SD23_BPDPK
Isoform
PDB entities 5
Chains and sequence ranges Author chain 1; PDBConstruct 1–298; UniProt 1–298 Author chain 2; PDBConstruct 1–298; UniProt 1–298 Author chain 3; PDBConstruct 1–298; UniProt 1–298 Author chain 4; PDBConstruct 1–298; UniProt 1–298 Author chain 5; PDBConstruct 1–298; UniProt 1–298 Author chain 6; PDBConstruct 1–298; UniProt 1–298

PHIKZ157

OrganismNot specified

UniProt Q8SD05

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 × 23 PDB declaration: 23-meric(23) Consistent with protein copy count Chain J; UniProt 1–445 Chain N; UniProt 1–445 Chain P; UniProt 1–445 Chain R; UniProt 1–445 Chain T; UniProt 1–445 Chain V; UniProt 1–445 Not recorded PHIKZ026 × 6 (Q8SDD6) PHIKZ027 × 2 (Q8SDD5) PHIKZ127 × 1 (Q8SD35) PHIKZ130 × 2 (Q8SD32) PHIKZ139 × 6 (Q8SD23) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.53 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8SD05_BPDPK
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–445; UniProt 1–445 Author chain N; PDBConstruct 1–445; UniProt 1–445 Author chain P; PDBConstruct 1–445; UniProt 1–445 Author chain R; PDBConstruct 1–445; UniProt 1–445 Author chain T; PDBConstruct 1–445; UniProt 1–445 Author chain V; PDBConstruct 1–445; UniProt 1–445

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 9xqd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xqd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9xqd
Deposition date deposition_date2025-11-18
Structure title titleThe structure of outer peripheral region in the phage phiKZ baseplate complex
Keywords keywordsbaseplate, outer peripheral, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier98.46
Radius of gyration Rg (electron density) rg_electron98.62
Forward intensity I(0) i013629500000.00
Molecular weight molecular_weight1007300.0 kDa
Excluded volume excluded_volume1264000 ų
Envelope volume envelope_volume2460500 ų
Hydration-shell volume shell_volume216840 ų
Envelope diameter envelope_diameter336.2
Shell Rg shell_rg87.33
Envelope Rg envelope_rg93.45
Shape Rg shape_rg98.61
Total Rg total_rg98.56
Total atoms total_atoms71157
Residues n_residues8852
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 dmax262.3
Rg (real space) rg_real94.66
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.3060e+10
I(0) uncertainty (real space) i0_real_error2.6290e+08
Rg (reciprocal space) rg_reciprocal97.51
I(0) (reciprocal space) i0_reciprocal13580000000.0000
Solution quality estimate total_estimate0.9149
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary114.8
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.8945
Highest regularization parameter α highest_alpha403000000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 1.000; Stabil: 0.969; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)