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8fxx

Cryo-EM structure of cowpox virus M2 in complex with human B7.2 (heptameric ring)

Method: ELECTRON MICROSCOPY Dmax: 174.0 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 × 14 PDB declaration: tetradecameric（14） Consistent with protein copy count Chain A； UniProt 18–218 Chain B； UniProt 18–218 Chain D； UniProt 18–218 Chain F； UniProt 18–218 Chain I； UniProt 18–218 Chain K； UniProt 18–218 Chain M； UniProt 18–218 Not recorded T-lymphocyte activation antigen CD86 × 7 （P42081） 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

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 8FXX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8FXW Cryo-EM structure of cowpox virus M2 in complex with human B7.1 (hexameric 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 × 12 PDB declaration: dodecameric
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）
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 2.70 Å
8FXY Cryo-EM structure of cowpox virus M2 in complex with human B7.2 (hexameric 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 × 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 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 4–204； UniProt 18–218 Author chain B； PDBConstruct 4–204； UniProt 18–218 Author chain D； PDBConstruct 4–204； UniProt 18–218 Author chain F； PDBConstruct 4–204； UniProt 18–218 Author chain I； PDBConstruct 4–204； UniProt 18–218 Author chain K； PDBConstruct 4–204； UniProt 18–218 Author chain M； PDBConstruct 4–204； UniProt 18–218

T-lymphocyte activation antigen CD86

Homo sapiens

UniProt P42081

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 26–134 Chain E； UniProt 26–134 Chain G； UniProt 26–134 Chain H； UniProt 26–134 Chain J； UniProt 26–134 Chain L； UniProt 26–134 Chain N； UniProt 26–134 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 3.26 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 8FXX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1I85 CRYSTAL STRUCTURE OF THE CTLA-4/B7-2 COMPLEX Deposited 2001-03-12 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 × 4 PDB declaration: tetrameric
Chain A 26–134（109 aa） Fragment：IG V-TYPE (RECEPTOR BINDING) DOMAIN
Chain B 26–134（109 aa） Fragment：IG V-TYPE (RECEPTOR BINDING) DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；PEG20K, HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.20 Å R-free 0.300
1NCN the receptor-binding domain of human B7-2 Deposited 2002-12-05 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 26–134（109 aa） Fragment：Ig V-type domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG4000, NaAC, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.70 Å R-free 0.278
1NCN the receptor-binding domain of human B7-2 Deposited 2002-12-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 26–134（109 aa） Fragment：Ig V-type domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG4000, NaAC, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.70 Å R-free 0.278
5YXK High resolution crystal structure of Human B7-2 IgV domain in P21 space group Deposited 2017-12-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–134（109 aa） Fragment：Ig-like V-type
Chain B 26–134（109 aa） Fragment：Ig-like V-type
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.1M Tris HCl pH 8.5, 2.4M Ammonium phosphate dibasic
Resolution 1.90 Å R-free 0.248
5YXK High resolution crystal structure of Human B7-2 IgV domain in P21 space group Deposited 2017-12-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 26–134（109 aa） Fragment：Ig-like V-type
Chain D 26–134（109 aa） Fragment：Ig-like V-type
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.1M Tris HCl pH 8.5, 2.4M Ammonium phosphate dibasic
Resolution 1.90 Å R-free 0.248
8FXY Cryo-EM structure of cowpox virus M2 in complex with human B7.2 (hexameric 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 × 12 PDB declaration: dodecameric
Chain C 26–243（218 aa）
Chain E 26–243（218 aa）
Chain G 26–243（218 aa）
Chain H 26–243（218 aa）
Chain J 26–243（218 aa）
Chain L 26–243（218 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
8HXB Cryo-EM structure of MPXV M2 hexamer in complex with human B7.2 Deposited 2023-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain G 26–238（213 aa）
Chain H 26–238（213 aa）
Chain I 26–238（213 aa）
Chain J 26–238（213 aa）
Chain K 26–238（213 aa）
Chain L 26–238（213 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
8HXC Cryo-EM structure of MPXV M2 heptamer in complex with human B7.2 Deposited 2023-01-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain H 26–238（213 aa）
Chain I 26–238（213 aa）
Chain J 26–238（213 aa）
Chain K 26–238（213 aa）
Chain L 26–238（213 aa）
Chain M 26–238（213 aa）
Chain N 26–238（213 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.12 Å

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD86_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 2–110； UniProt 26–134 Author chain E； PDBConstruct 2–110； UniProt 26–134 Author chain G； PDBConstruct 2–110； UniProt 26–134 Author chain H； PDBConstruct 2–110； UniProt 26–134 Author chain J； PDBConstruct 2–110； UniProt 26–134 Author chain L； PDBConstruct 2–110； UniProt 26–134 Author chain N； PDBConstruct 2–110； UniProt 26–134

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 8fxx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fxx
Deposition date deposition_date2023-01-25
Structure title titleCryo-EM structure of cowpox virus M2 in complex with human B7.2 (heptameric ring)
Keywords keywords;poxvirus M2 protein, OPG038, T-cell costimulation, poxviral immune evasion domain PIE, B7.1, Structural Genomics, 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_guinier62.73 Å
Radius of gyration Rg (electron density) rg_electron62.33 Å
Forward intensity I(0) i0923816000.00
Molecular weight molecular_weight250810.0 kDa
Excluded volume excluded_volume311130 ų
Envelope volume envelope_volume534980 ų
Hydration-shell volume shell_volume70034 ų
Envelope diameter envelope_diameter178.2 Å
Shell Rg shell_rg70.10 Å
Envelope Rg envelope_rg58.29 Å
Shape Rg shape_rg62.38 Å
Total Rg total_rg62.35 Å
Total atoms total_atoms17556
Residues n_residues2142
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 dmax174.0 Å
Rg (real space) rg_real62.50 Å
Rg uncertainty (real space) rg_real_error1.50 Å
I(0) (real space) i0_real9.2380e+08
I(0) uncertainty (real space) i0_real_error1.8120e+07
Rg (reciprocal space) rg_reciprocal62.86 Å
I(0) (reciprocal space) i0_reciprocal924300000.0000
Solution quality estimate total_estimate0.8350
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary104.4 Å
Skewness Skewness skewness-0.068
Kurtosis Kurtosis kurtosis-0.880
Angular range angular_range— – 0.1250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17550000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.000
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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)