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8fxw

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

Method: ELECTRON MICROSCOPY Dmax: 164.3 Å Quality: GOOD
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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 × 12 PDB declaration: dodecameric（12） 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 Not recorded T-lymphocyte activation antigen CD80 × 6 （P33681） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4；150 mM Nacl, 25 mM HEPES, pH7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.70 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.

Other PDB Difference from Current Entry 8FXW Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8FXX Cryo-EM structure of cowpox virus M2 in complex with human B7.2 (heptameric ring) Deposited 2023-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain A 18–218（201 aa）
Chain B 18–218（201 aa）
Chain D 18–218（201 aa）
Chain F 18–218（201 aa）
Chain I 18–218（201 aa）
Chain K 18–218（201 aa）
Chain M 18–218（201 aa）
Not recorded 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 3.26 Å
8FXY Cryo-EM structure of cowpox virus M2 in complex with human B7.2 (hexameric ring) Deposited 2023-01-25 Different construct Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 18–218（201 aa）
Chain B 18–218（201 aa）
Chain D 18–218（201 aa）
Chain F 18–218（201 aa）
Chain I 18–218（201 aa）
Chain K 18–218（201 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；150 mM Nacl, 25 mM HEPES, pH7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.34 Å
8FXZ Cryo-EM structure of cowpox virus M2 in complex with human B7.1 (heptameric ring) Deposited 2023-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain A 18–220（203 aa）
Chain B 18–220（203 aa）
Chain D 18–220（203 aa）
Chain F 18–220（203 aa）
Chain I 18–220（203 aa）
Chain K 18–220（203 aa）
Chain M 18–220（203 aa）
Not recorded 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

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

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 × 12 PDB declaration: dodecameric（12） 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 Not recorded CPXV040 protein × 6 （Q8QN22） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4；150 mM Nacl, 25 mM HEPES, pH7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.70 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.

Other PDB Difference from Current Entry 8FXW Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1DR9 CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80) Deposited 2000-01-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–234（200 aa） Fragment：EXTRACELLULAR REGION
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG400, Na Hepes, CaCl2, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 20K
Resolution 3.00 Å R-free 0.280
1I8L HUMAN B7-1/CTLA-4 CO-STIMULATORY COMPLEX Deposited 2001-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 35–242（208 aa） Fragment：EXTRACELLULAR DOMAIN, RESIDUES 35-242
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 MAN alpha-D-mannopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；298 K；16% PEG 8000, 0.1M CACODYLATE, PH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 3.00 Å R-free 0.257
1I8L HUMAN B7-1/CTLA-4 CO-STIMULATORY COMPLEX Deposited 2001-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 35–242（208 aa） Fragment：EXTRACELLULAR DOMAIN, RESIDUES 35-242
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 MAN alpha-D-mannopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；298 K；16% PEG 8000, 0.1M CACODYLATE, PH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 3.00 Å R-free 0.257
7TPS Crystal structure of ALPN-202 (engineered CD80 vIgD) in complex with PD-L1 Deposited 2022-01-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 35–140（106 aa）
Mutation：H52Y, A60E, E69D, M81L, V102M, A105G, D124G NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.03 M sodium nitrate, 0.03 M sodium phosphate dibasic, 0.03 M ammonium sulfate, 0.1 M sodium HEPES/MOPS (acid), pH 7.5, 20% v/v glycerol, 10% w/v PEG 4000
Resolution 3.15 Å R-free 0.291
7TPS Crystal structure of ALPN-202 (engineered CD80 vIgD) in complex with PD-L1 Deposited 2022-01-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 35–140（106 aa）
Mutation：H52Y, A60E, E69D, M81L, V102M, A105G, D124G NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.03 M sodium nitrate, 0.03 M sodium phosphate dibasic, 0.03 M ammonium sulfate, 0.1 M sodium HEPES/MOPS (acid), pH 7.5, 20% v/v glycerol, 10% w/v PEG 4000
Resolution 3.15 Å R-free 0.291
8FXZ Cryo-EM structure of cowpox virus M2 in complex with human B7.1 (heptameric ring) Deposited 2023-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain C 35–235（201 aa）
Chain E 35–235（201 aa）
Chain G 35–235（201 aa）
Chain H 35–235（201 aa）
Chain J 35–235（201 aa）
Chain L 35–235（201 aa）
Chain N 35–235（201 aa）
Not recorded 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
8HXA Cryo-EM structure of MPXV M2 in complex with human B7.1 Deposited 2023-01-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain G 35–234（200 aa）
Chain H 35–234（200 aa）
Chain I 35–234（200 aa）
Chain J 35–234（200 aa）
Chain K 35–234（200 aa）
Chain L 35–234（200 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.04 Å

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

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 8fxw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fxw
Deposition date deposition_date2023-01-25
Structure title titleCryo-EM structure of cowpox virus M2 in complex with human B7.1 (hexameric ring)
Keywords keywords;poxvirus M2 protein, OPG038, T-cell costimulation, poxviral immune evasion domain PIE, B7.1, Structural Genomics, Center for Structural Genomics of Infectious Diseases, CSGID, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier55.23 Å
Radius of gyration Rg (electron density) rg_electron55.27 Å
Forward intensity I(0) i0686025000.00
Molecular weight molecular_weight216520.0 kDa
Excluded volume excluded_volume269440 ų
Envelope volume envelope_volume423990 ų
Hydration-shell volume shell_volume62248 ų
Envelope diameter envelope_diameter165.0 Å
Shell Rg shell_rg62.35 Å
Envelope Rg envelope_rg52.90 Å
Shape Rg shape_rg55.26 Å
Total Rg total_rg55.50 Å
Total atoms total_atoms29916
Residues n_residues1854
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax164.3 Å
Rg (real space) rg_real55.10 Å
Rg uncertainty (real space) rg_real_error1.26 Å
I(0) (real space) i0_real6.8600e+08
I(0) uncertainty (real space) i0_real_error1.4420e+07
Rg (reciprocal space) rg_reciprocal55.30 Å
I(0) (reciprocal space) i0_reciprocal686200000.0000
Solution quality estimate total_estimate0.8442
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.3 Å
Skewness Skewness skewness0.017
Kurtosis Kurtosis kurtosis-0.787
Angular range angular_range— – 0.1400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14810000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.089
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)