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High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility

Analyse High resolution cryo EM analysis of HPV16 identifies minor structural protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KZF
Type
protein
Length
2,864 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major capsid protein L1
UniProt
P03101
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 5 distinct chains · 11% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
FMajor capsid protein L1protein48311% helix, 35% strandP03101
BMajor capsid protein L1protein46611% helix, 35% strandP03101
C, DMajor capsid protein L1protein48010% helix, 33% strandP03101
EMajor capsid protein L1protein48112% helix, 33% strandP03101
AMajor capsid protein L1protein47411% helix, 30% strandP03101

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111420.800.82143empty
29860.700.7552empty
34690.680.7973empty
44750.680.7962empty
54580.680.7969empty

Interfaces

12 interfaces between chains.

  • B–C · 4156 Ų buried · 55 hydrogen bonds · protein-protein
  • F–E · 4153 Ų buried · 54 hydrogen bonds · protein-protein
  • C–D · 3988 Ų buried · 58 hydrogen bonds · protein-protein
  • F–B · 3971 Ų buried · 56 hydrogen bonds · protein-protein
  • D–E · 3915 Ų buried · 61 hydrogen bonds · protein-protein

Compared structures

  • 7KZF · High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and… · the same entry in another collection · chain F against F, TM-score 1.00

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