7m22

Cryo-EM structure of the HCMV pentamer bound by human neuropilin 2

Method: ELECTRON MICROSCOPY Dmax: 111.9 Å Quality: GOOD

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

Envelope protein UL128

Human cytomegalovirus

UniProt C8BLJ3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 28–171 Not recorded Envelope glycoprotein UL130 × 1 (A0A0G2TB82) UL131A × 1 (Q38M21) Neuropilin-2 × 1 (O60462) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Grid was blotted with a force of -6 for 3 seconds Resolution 3.65 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C8BLJ3_HCMV
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–144; UniProt 28–171

Envelope glycoprotein UL130

Human cytomegalovirus

UniProt A0A0G2TB82

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 26–214 Not recorded Envelope protein UL128 × 1 (C8BLJ3) UL131A × 1 (Q38M21) Neuropilin-2 × 1 (O60462) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Grid was blotted with a force of -6 for 3 seconds Resolution 3.65 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 A0A0G2TB82_HCMV
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–189; UniProt 26–214

UL131A

Human cytomegalovirus

UniProt Q38M21

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 19–129 Not recorded Envelope protein UL128 × 1 (C8BLJ3) Envelope glycoprotein UL130 × 1 (A0A0G2TB82) Neuropilin-2 × 1 (O60462) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Grid was blotted with a force of -6 for 3 seconds Resolution 3.65 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q38M21_HCMV
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–111; UniProt 19–129

Neuropilin-2

Homo sapiens

UniProt O60462

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N; UniProt 23–595 Not recorded Envelope protein UL128 × 1 (C8BLJ3) Envelope glycoprotein UL130 × 1 (A0A0G2TB82) UL131A × 1 (Q38M21) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Grid was blotted with a force of -6 for 3 seconds Resolution 3.65 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.

15 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NRP2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain N; PDBConstruct 1–573; UniProt 23–595

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 7m22

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7m22
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7m22
Deposition date deposition_date2021-03-15
Structure title titleCryo-EM structure of the HCMV pentamer bound by human neuropilin 2
Keywords keywordsHCMV pentamer, NRP2, cytomegalovirus, host receptor, VIRAL PROTEIN, VIRAL PROTEIN-HOST RECEPTOR complex; VIRAL PROTEIN/HOST RECEPTOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.84
Radius of gyration Rg (electron density) rg_electron31.26
Forward intensity I(0) i0121186000.00
Molecular weight molecular_weight85851.0 kDa
Excluded volume excluded_volume106920 ų
Envelope volume envelope_volume143880 ų
Hydration-shell volume shell_volume38785 ų
Envelope diameter envelope_diameter118.5
Shell Rg shell_rg37.70
Envelope Rg envelope_rg31.14
Shape Rg shape_rg31.26
Total Rg total_rg31.81
Total atoms total_atoms6042
Residues n_residues748
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 dmax111.9
Rg (real space) rg_real31.80
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.2120e+08
I(0) uncertainty (real space) i0_real_error1.9910e+06
Rg (reciprocal space) rg_reciprocal31.82
I(0) (reciprocal space) i0_reciprocal121200000.0000
Solution quality estimate total_estimate0.8713
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.3
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34990000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)