8fxz

Cryo-EM structure of cowpox virus M2 in complex with human B7.1 (heptameric ring)

Method: ELECTRON MICROSCOPY Dmax: 173.6 Å Quality: GOOD

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

CPXV040 protein

Cowpox virus (Brighton Red)

UniProt Q8QN22

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 18–220 Chain B; UniProt 18–220 Chain D; UniProt 18–220 Chain F; UniProt 18–220 Chain I; UniProt 18–220 Chain K; UniProt 18–220 Chain M; UniProt 18–220 Not recorded T-lymphocyte activation antigen CD80 × 7 (P33681) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;150 mM Nacl, 25 mM HEPES, pH7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8QN22_CWPXB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–206; UniProt 18–220 Author chain B; PDBConstruct 4–206; UniProt 18–220 Author chain D; PDBConstruct 4–206; UniProt 18–220 Author chain F; PDBConstruct 4–206; UniProt 18–220 Author chain I; PDBConstruct 4–206; UniProt 18–220 Author chain K; PDBConstruct 4–206; UniProt 18–220 Author chain M; PDBConstruct 4–206; UniProt 18–220

T-lymphocyte activation antigen CD80

Homo sapiens

UniProt P33681

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain C; UniProt 35–235 Chain E; UniProt 35–235 Chain G; UniProt 35–235 Chain H; UniProt 35–235 Chain J; UniProt 35–235 Chain L; UniProt 35–235 Chain N; UniProt 35–235 Not recorded CPXV040 protein × 7 (Q8QN22) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;150 mM Nacl, 25 mM HEPES, pH7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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.

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

View Construct and Data Evidence
UniProt name CD80_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–201; UniProt 35–235 Author chain E; PDBConstruct 1–201; UniProt 35–235 Author chain G; PDBConstruct 1–201; UniProt 35–235 Author chain H; PDBConstruct 1–201; UniProt 35–235 Author chain J; PDBConstruct 1–201; UniProt 35–235 Author chain L; PDBConstruct 1–201; UniProt 35–235 Author chain N; PDBConstruct 1–201; UniProt 35–235

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 8fxz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fxz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fxz
Deposition date deposition_date2023-01-25
Structure title titleCryo-EM structure of cowpox virus M2 in complex with human B7.1 (heptameric ring)
Keywords keywords;poxvirus M2 protein, OPG038, T-cell costimulation, poxviral immune evasion domain PIE, B7.2, Structural Genomics, CSGID, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.04
Radius of gyration Rg (electron density) rg_electron62.01
Forward intensity I(0) i0924186000.00
Molecular weight molecular_weight252730.0 kDa
Excluded volume excluded_volume314440 ų
Envelope volume envelope_volume531710 ų
Hydration-shell volume shell_volume69497 ų
Envelope diameter envelope_diameter177.2
Shell Rg shell_rg70.32
Envelope Rg envelope_rg58.33
Shape Rg shape_rg62.00
Total Rg total_rg62.21
Total atoms total_atoms34909
Residues n_residues2163
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 dmax173.6
Rg (real space) rg_real61.82
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real9.2420e+08
I(0) uncertainty (real space) i0_real_error1.6980e+07
Rg (reciprocal space) rg_reciprocal62.17
I(0) (reciprocal space) i0_reciprocal924700000.0000
Solution quality estimate total_estimate0.8365
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary104.1
Skewness Skewness skewness-0.065
Kurtosis Kurtosis kurtosis-0.883
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18260000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)