7m30

Cryo-EM structure of the HCMV pentamer bound by antibodies 1-103, 1-32 and 2-25

Method: ELECTRON MICROSCOPY Dmax: 136.1 Å Quality: REASONABLE

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

Envelope glycoprotein L

Human cytomegalovirus

UniProt P16832

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 31–278 Not recorded Envelope protein UL128 × 1 (C8BLJ3) Envelope glycoprotein UL130 × 1 (A0A0G2TB82) UL131A × 1 (Q38M21) 2-25 Fab Heavy Chain × 1 2-25 Fab Light Chain × 1 1-32 Fab Heavy Chain × 1 1-32 Fab Light Chain × 1 1-103 Fab Heavy Chain × 1 1-103 Fab Light Chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for six seconds with a force of "1" before plunging Resolution 3.81 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GL_HCMVA
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–248; UniProt 31–278

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 28–171 Not recorded Envelope glycoprotein L × 1 (P16832) Envelope glycoprotein UL130 × 1 (A0A0G2TB82) UL131A × 1 (Q38M21) 2-25 Fab Heavy Chain × 1 2-25 Fab Light Chain × 1 1-32 Fab Heavy Chain × 1 1-32 Fab Light Chain × 1 1-103 Fab Heavy Chain × 1 1-103 Fab Light Chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for six seconds with a force of "1" before plunging Resolution 3.81 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 2
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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 26–214 Not recorded Envelope glycoprotein L × 1 (P16832) Envelope protein UL128 × 1 (C8BLJ3) UL131A × 1 (Q38M21) 2-25 Fab Heavy Chain × 1 2-25 Fab Light Chain × 1 1-32 Fab Heavy Chain × 1 1-32 Fab Light Chain × 1 1-103 Fab Heavy Chain × 1 1-103 Fab Light Chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for six seconds with a force of "1" before plunging Resolution 3.81 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 3
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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 19–129 Not recorded Envelope glycoprotein L × 1 (P16832) Envelope protein UL128 × 1 (C8BLJ3) Envelope glycoprotein UL130 × 1 (A0A0G2TB82) 2-25 Fab Heavy Chain × 1 2-25 Fab Light Chain × 1 1-32 Fab Heavy Chain × 1 1-32 Fab Light Chain × 1 1-103 Fab Heavy Chain × 1 1-103 Fab Light Chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for six seconds with a force of "1" before plunging Resolution 3.81 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 4
Chains and sequence ranges Author chain E; PDBConstruct 1–111; UniProt 19–129

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 7m30

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7m30
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7m30
Deposition date deposition_date2021-03-17
Structure title titleCryo-EM structure of the HCMV pentamer bound by antibodies 1-103, 1-32 and 2-25
Keywords keywordsHCMV pentamer, Fab, cytomegalovirus, immunocomplex, 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_guinier42.59
Radius of gyration Rg (electron density) rg_electron42.26
Forward intensity I(0) i0265810000.00
Molecular weight molecular_weight130580.0 kDa
Excluded volume excluded_volume162130 ų
Envelope volume envelope_volume237480 ų
Hydration-shell volume shell_volume47139 ų
Envelope diameter envelope_diameter140.7
Shell Rg shell_rg47.84
Envelope Rg envelope_rg40.44
Shape Rg shape_rg42.24
Total Rg total_rg42.60
Total atoms total_atoms9191
Residues n_residues1145
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 dmax136.1
Rg (real space) rg_real42.47
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real2.6580e+08
I(0) uncertainty (real space) i0_real_error4.5520e+06
Rg (reciprocal space) rg_reciprocal42.59
I(0) (reciprocal space) i0_reciprocal265800000.0000
Solution quality estimate total_estimate0.6627
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.5
Skewness Skewness skewness0.045
Kurtosis Kurtosis kurtosis-0.704
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15440000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 0.016; Positv: 1.000; Valcen: 0.994; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7m30F01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7m30G01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7m30H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7m30L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7m30M01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7m30N01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)