7t4s

CryoEM structure of the HCMV Pentamer gH/gL/UL128/UL130/UL131A in complex with NRP2 and neutralizing fabs 8I21 and 13H11

Method: ELECTRON MICROSCOPY Dmax: 215.6 Å Quality: GOOD

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

Envelope glycoprotein H

Human betaherpesvirus 5

UniProt F5H9T3

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–715 Not recorded Envelope glycoprotein L × 1 (Q71DN9) Envelope protein UL128 × 1 (Q38LY2) Envelope glycoprotein UL130 × 1 (Q38M07) Envelope protein UL131A × 1 (Q8AZ45) Neuropilin-2 × 1 (O60462) Fab 8I21 heavy chain × 1 Fab 13H11 heavy chain × 1 Fab 13H11 light chain × 1 Fab 8I21 light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds before plunging Resolution 3.10 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 F5H9T3_HCMV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–715; UniProt 1–715

Envelope glycoprotein L

Human betaherpesvirus 5

UniProt Q71DN9

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 1–278 Not recorded Envelope glycoprotein H × 1 (F5H9T3) Envelope protein UL128 × 1 (Q38LY2) Envelope glycoprotein UL130 × 1 (Q38M07) Envelope protein UL131A × 1 (Q8AZ45) Neuropilin-2 × 1 (O60462) Fab 8I21 heavy chain × 1 Fab 13H11 heavy chain × 1 Fab 13H11 light chain × 1 Fab 8I21 light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds before plunging Resolution 3.10 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 Q71DN9_HCMV
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–278; UniProt 1–278

Envelope protein UL128

Human betaherpesvirus 5

UniProt Q38LY2

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–171 Not recorded Envelope glycoprotein H × 1 (F5H9T3) Envelope glycoprotein L × 1 (Q71DN9) Envelope glycoprotein UL130 × 1 (Q38M07) Envelope protein UL131A × 1 (Q8AZ45) Neuropilin-2 × 1 (O60462) Fab 8I21 heavy chain × 1 Fab 13H11 heavy chain × 1 Fab 13H11 light chain × 1 Fab 8I21 light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds before plunging Resolution 3.10 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 Q38LY2_HCMV
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–171; UniProt 1–171

Envelope glycoprotein UL130

Human betaherpesvirus 5

UniProt Q38M07

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 1–214 Not recorded Envelope glycoprotein H × 1 (F5H9T3) Envelope glycoprotein L × 1 (Q71DN9) Envelope protein UL128 × 1 (Q38LY2) Envelope protein UL131A × 1 (Q8AZ45) Neuropilin-2 × 1 (O60462) Fab 8I21 heavy chain × 1 Fab 13H11 heavy chain × 1 Fab 13H11 light chain × 1 Fab 8I21 light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds before plunging Resolution 3.10 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 Q38M07_HCMV
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–214; UniProt 1–214

Envelope protein UL131A

Human betaherpesvirus 5

UniProt Q8AZ45

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 1–129 Not recorded Envelope glycoprotein H × 1 (F5H9T3) Envelope glycoprotein L × 1 (Q71DN9) Envelope protein UL128 × 1 (Q38LY2) Envelope glycoprotein UL130 × 1 (Q38M07) Neuropilin-2 × 1 (O60462) Fab 8I21 heavy chain × 1 Fab 13H11 heavy chain × 1 Fab 13H11 light chain × 1 Fab 8I21 light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds before plunging Resolution 3.10 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 Q8AZ45_HCMV
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–129; UniProt 1–129

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain F; UniProt 1–864 Not recorded Envelope glycoprotein H × 1 (F5H9T3) Envelope glycoprotein L × 1 (Q71DN9) Envelope protein UL128 × 1 (Q38LY2) Envelope glycoprotein UL130 × 1 (Q38M07) Envelope protein UL131A × 1 (Q8AZ45) Fab 8I21 heavy chain × 1 Fab 13H11 heavy chain × 1 Fab 13H11 light chain × 1 Fab 8I21 light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds before plunging Resolution 3.10 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–864; UniProt 1–864

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 7t4s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7t4s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7t4s
Deposition date deposition_date2021-12-10
Structure title titleCryoEM structure of the HCMV Pentamer gH/gL/UL128/UL130/UL131A in complex with NRP2 and neutralizing fabs 8I21 and 13H11
Keywords keywordsglycoprotein complex, antibody complex, Neuropilin 2, VIRAL PROTEIN, VIRAL PROTEIN-Immune System complex; VIRAL PROTEIN/Immune System
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.68
Radius of gyration Rg (electron density) rg_electron61.17
Forward intensity I(0) i0756824000.00
Molecular weight molecular_weight232890.0 kDa
Excluded volume excluded_volume292070 ų
Envelope volume envelope_volume443690 ų
Hydration-shell volume shell_volume62317 ų
Envelope diameter envelope_diameter212.2
Shell Rg shell_rg60.63
Envelope Rg envelope_rg58.94
Shape Rg shape_rg61.13
Total Rg total_rg61.31
Total atoms total_atoms16404
Residues n_residues2045
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 dmax215.6
Rg (real space) rg_real61.17
Rg uncertainty (real space) rg_real_error3.09
I(0) (real space) i0_real7.5680e+08
I(0) uncertainty (real space) i0_real_error1.4490e+07
Rg (reciprocal space) rg_reciprocal60.20
I(0) (reciprocal space) i0_reciprocal755600000.0000
Solution quality estimate total_estimate0.7561
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.5
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.710
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26270000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.674; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.804; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7t4sF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like

8. Citations (1)

9. Files and Curves (10)