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Cryo-EM structure of bacteriophage lambda procapsid at 5.03 ångström

Analyse Cryo-EM structure of bacteriophage lambda procapsid at 5.03 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VI9
Type
protein
Length
2,345 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major capsid protein
UniProt
P03713
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 22% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GMajor capsid proteinprotein33522% helix, 23% strandP03713

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17170.830.8691empty
210640.810.83137empty
310360.810.82109empty
43760.800.8964empty
58600.790.8296empty

Interfaces

11 interfaces between chains.

  • D–E · 2143 Ų buried · 28 hydrogen bonds · protein-protein
  • A–F · 2062 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 2034 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 2020 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 1981 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 7VI9 · Cryo-EM structure of bacteriophage lambda procapsid at 5.03 Angstrom · the same entry in another collection · chain A against A, TM-score 1.00

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