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High-resolution structure analysis of antibody V5 conformational epitope on human papillomavirus 16

Analyse High-resolution structure analysis of antibody V5 conformational epitope on… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BT3
Type
protein
Length
4,572 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
V5 Fab light-chain; V5 Fab heavy-chain; Major capsid protein L1
UniProt
P03101
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 6 distinct chains · 10% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GV5 Fab light-chainprotein2206% helix, 40% strand—
B, D, F, HV5 Fab heavy-chainprotein2230% helix, 39% strand—
I, L, NMajor capsid protein L1protein46812% helix, 30% strandP03101
JMajor capsid protein L1protein46012% helix, 29% strandP03101
KMajor capsid protein L1protein46912% helix, 28% strandP03101
MMajor capsid protein L1protein46712% helix, 28% strandP03101

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18830.840.85118empty
210220.840.84135empty
39000.830.85119empty
49360.810.83105empty
56060.800.8590empty

Interfaces

42 interfaces between chains.

  • J–K · 3718 Ų buried · 29 hydrogen bonds · protein-protein
  • L–M · 3696 Ų buried · 28 hydrogen bonds · protein-protein
  • K–L · 3656 Ų buried · 34 hydrogen bonds · protein-protein
  • M–N · 3589 Ų buried · 28 hydrogen bonds · protein-protein
  • J–N · 3538 Ų buried · 30 hydrogen bonds · protein-protein

Compared structures

  • 6BT3 · High-Resolution Structure Analysis of Antibody V5 Conformational Epitope on Human… · the same entry in another collection · chain A against A, TM-score 1.00

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