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Quasi-atomic resolution model of bacteriophage PRD1 SUS607 mutant, obtained by combined cryo-EM and X-ray crystallography.

Analyse Quasi-atomic resolution model of bacteriophage PRD1 SUS607 mutant, obtained by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GW8
Type
protein
Length
4,451 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major capsid protein
UniProt
P22535
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 4 distinct chains · 15% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, G, JMajor capsid proteinprotein37014% helix, 42% strandP22535
B, E, H, KMajor capsid proteinprotein37215% helix, 42% strandP22535
C, F, I, LMajor capsid proteinprotein37116% helix, 43% strandP22535
DMajor capsid proteinprotein36914% helix, 42% strandP22535

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111470.850.86114empty
211140.790.81107empty
36480.780.8365empty
49040.770.8085empty
55040.770.8443empty

Interfaces

22 interfaces between chains.

  • A–C · 1782 Ų buried · 33 hydrogen bonds · protein-protein
  • G–I · 1779 Ų buried · 33 hydrogen bonds · protein-protein
  • D–F · 1776 Ų buried · 33 hydrogen bonds · protein-protein
  • J–L · 1774 Ų buried · 33 hydrogen bonds · protein-protein
  • H–I · 1769 Ų buried · 36 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 isopeptide (isopeptide).

Compared structures

  • 1GW8 · quasi-atomic resolution model of bacteriophage PRD1 sus607 mutant, obtained by combined… · the same entry in another collection · chain A against A, TM-score 1.00

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