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MolNFT v1 · #167506 · protein

A 2.8 ångström cryo-EM structure of a glycoprotein B-neutralizing antibody complex reveals a critical domain for herpesvirus fusion initiation

6VN1 · Human monoclonal antibody 93K variable light chain: “A 2.8 ångström cryo-EM structure of a glycoprotein B-neutralizing antibody complex reveals a critical domain…”. Electron microscopy, 20 pockets (best druggability 0.82). MolNFT v1…

PDB
6VN1
Type
protein
Length
2,454 residues
Chains
9
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Human monoclonal antibody 93K variable light chain; Human monoclonal antibody 93K…
UniProt
A0A1B1JGG9
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 3 distinct chains · 14% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
L, M, NHuman monoclonal antibody 93K variable light chainprotein1060% helix, 24% strand—
H, I, JHuman monoclonal antibody 93K variable heavy chainprotein1285% helix, 30% strand—
A, B, CEnvelope glycoprotein Bprotein58419% helix, 36% strandA0A1B1JGG9

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111630.820.83105empty
2940.780.9825empty
31280.710.9225empty
45860.710.8072empty
51280.710.9126empty

Interfaces

12 interfaces between chains.

  • A–C · 6666 Ų buried · 75 hydrogen bonds · protein-protein
  • B–C · 6662 Ų buried · 78 hydrogen bonds · protein-protein
  • A–B · 6658 Ų buried · 77 hydrogen bonds · protein-protein
  • N–J · 926 Ų buried · 6 hydrogen bonds · protein-protein
  • L–H · 920 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 21 disulfide (disulfide).

Compared structures

  • 6VN1 · A 2.8 Angstrom Cryo-EM Structure of a Glycoprotein B-Neutralizing Antibody Complex… · the same entry in another collection · chain L against L, TM-score 1.00

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