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Structure of 2A protein from encephalomyocarditis virus (emcv)

Analyse Structure of 2A protein from encephalomyocarditis virus (emcv) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BNY
Type
protein
Length
524 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Genome polyprotein
EC
3.6.4.13, 3.4.22.28, 2.7.7.48
UniProt
P12296
Ligands
SO4
Pockets
5 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 16% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGenome polyprotein (EC 3.6.4.13, 3.4.22.28, 2.7.7.48)protein13216% helix, 38% strandP12296
BGenome polyprotein (EC 3.6.4.13, 3.4.22.28, 2.7.7.48)protein14015% helix, 37% strandP12296
C, DGenome polyprotein (EC 3.6.4.13, 3.4.22.28, 2.7.7.48)protein12617% helix, 40% strandP12296

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 9 copies · chains A, D, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.480.8016empty
2680.410.8024empty
31380.370.7318empty
41250.360.7319empty
5570.280.7414empty

Interfaces

5 interfaces between chains.

  • A–D · 753 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 717 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 676 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 323 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 79 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 7BNY · Structure of 2A protein from encephalomyocarditis virus (EMCV) · the same entry in another collection · chain A against A, TM-score 1.00

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