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Pentamer structure of major capsid protein L1 of human papilloma virus type 11

Analyse Pentamer structure of major capsid protein L1 of human papilloma virus type 11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2R5K
Type
protein
Length
2,095 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major capsid protein L1
UniProt
P04012
Pockets
20 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EMajor capsid protein L1protein41914% helix, 38% strandP04012

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110100.700.7454empty
23210.620.7952empty
33430.610.7853empty
43540.610.7752empty
52810.610.7951empty

Interfaces

10 interfaces between chains.

  • D–E · 3555 Ų buried · 63 hydrogen bonds · protein-protein
  • C–D · 3550 Ų buried · 64 hydrogen bonds · protein-protein
  • A–B · 3548 Ų buried · 60 hydrogen bonds · protein-protein
  • A–E · 3537 Ų buried · 59 hydrogen bonds · protein-protein
  • B–C · 3531 Ų buried · 60 hydrogen bonds · protein-protein

Compared structures

  • 2R5K · Pentamer Structure of Major Capsid protein L1 of Human Papilloma Virus type 11 · the same entry in another collection · chain A against A, TM-score 1.00

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