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KAPOSI'S sarcoma-associated herpesvirus (kshv), C12 portal dodecamer structure

Analyse KAPOSI'S sarcoma-associated herpesvirus (kshv), C12 portal dodecamer structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PPI
Type
protein
Length
4,956 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Portal protein
UniProt
Q76RH0
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 53% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LPortal proteinprotein41353% helix, 9% strandQ76RH0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17000.850.8863empty
28680.840.8672empty
39540.830.8586empty
49690.830.8488empty
59540.830.8485empty

Interfaces

24 interfaces between chains.

  • C–D · 4044 Ų buried · 30 hydrogen bonds · protein-protein
  • A–L · 4044 Ų buried · 32 hydrogen bonds · protein-protein
  • K–L · 4039 Ų buried · 30 hydrogen bonds · protein-protein
  • B–C · 4036 Ų buried · 30 hydrogen bonds · protein-protein
  • G–H · 4036 Ų buried · 30 hydrogen bonds · protein-protein

Compared structures

  • 6PPI · Kaposi's sarcoma-associated herpesvirus (KSHV), C12 portal dodecamer structure · the same entry in another collection · chain A against A, TM-score 1.00

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