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Quasi-atomic resolution model of bacteriophage PRD1 P3-shell, obtained by combined cryo-EM and X-ray crystallography.

Analyse Quasi-atomic resolution model of bacteriophage PRD1 P3-shell, obtained by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HB5
Type
protein
Length
3,345 residues
Chains
9
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bacteriophage PRD1 P3-shell
UniProt
P22535
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 3 distinct chains · 15% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, GBacteriophage PRD1 P3-shellprotein37014% helix, 43% strandP22535
B, E, HBacteriophage PRD1 P3-shellprotein37414% helix, 43% strandP22535
C, F, IBacteriophage PRD1 P3-shellprotein37116% helix, 43% strandP22535

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110310.860.8783empty
21630.780.9426empty
34980.770.8543empty
48810.770.8091empty
54910.760.8442empty

Interfaces

15 interfaces between chains.

  • E–F · 1873 Ų buried · 37 hydrogen bonds · protein-protein
  • B–C · 1868 Ų buried · 37 hydrogen bonds · protein-protein
  • H–I · 1865 Ų buried · 37 hydrogen bonds · protein-protein
  • A–C · 1793 Ų buried · 31 hydrogen bonds · protein-protein
  • D–F · 1790 Ų buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 isopeptide (isopeptide).

Compared structures

  • 1HB5 · quasi-atomic resolution model of bacteriophage PRD1 P3-shell, obtained by combined… · the same entry in another collection · chain A against A, TM-score 1.00

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