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Cryo-EM reconstruction of quasi-HPV16 complex with H16.1A Fab

Analyse Cryo-EM reconstruction of quasi-HPV16 complex with H16.1A Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3J8Z
Type
protein
Length
3,021 residues
Chains
13
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L1; H16.1A light chain; H16.1A heavy chain
UniProt
Q4VRM0
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 3 distinct chains · 12% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EL1protein42114% helix, 38% strandQ4VRM0
L, J, K, MH16.1A light chainprotein1153% helix, 50% strand—
H, F, G, IH16.1A heavy chainprotein11411% helix, 49% strand—

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14090.800.8871empty
27820.790.83102empty
38200.770.81115empty
48230.760.80105empty
58880.670.7462empty

Interfaces

32 interfaces between chains.

  • B–C · 3480 Ų buried · 62 hydrogen bonds · protein-protein
  • A–E · 3468 Ų buried · 66 hydrogen bonds · protein-protein
  • D–E · 3466 Ų buried · 64 hydrogen bonds · protein-protein
  • A–B · 3464 Ų buried · 64 hydrogen bonds · protein-protein
  • C–D · 3454 Ų buried · 66 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3J8Z · Cryo-EM reconstruction of quasi-HPV16 complex with H16.1A Fab · the same entry in another collection · chain A against A, TM-score 1.00

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