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The cryo-EM structure of coxsackievirus A16 a-particle

Analyse The cryo-EM structure of coxsackievirus A16 a-particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LHB
Type
protein
Length
648 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
VP1; VP2; VP3
EC
3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48
UniProt
A0A2S1BJ89, A0A1D3TZV2, A0A2R4NBT3
Pockets
10 · best druggability 0.61

Structure

electron microscopy · 3 distinct chains · 10% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVP1protein2127% helix, 30% strandA0A2S1BJ89
BVP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48)protein21011% helix, 36% strandA0A1D3TZV2
CVP3 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48)protein22611% helix, 35% strandA0A2R4NBT3

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12790.610.7949empty
21390.510.7921empty
31710.500.7723empty
41700.460.7618empty
51500.450.7627empty

Interfaces

3 interfaces between chains.

  • A–C · 3316 Ų buried · 48 hydrogen bonds · protein-protein
  • B–C · 1555 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 1355 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6LHB · The cryo-EM structure of coxsackievirus A16 A-particle · the same entry in another collection · chain C against C, TM-score 1.00

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