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Structure of the in vitro assembled bacteriophage PHI6 polymerase complex

Analyse Structure of the in vitro assembled bacteriophage PHI6 polymerase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5FJ5
Type
protein
Length
1,522 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major inner protein P1
UniProt
P11126
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 42% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMajor inner protein P1protein76142% helix, 3% strandP11126

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15740.820.8868empty
21420.790.9632empty
31460.780.9534empty
41110.780.9724empty
54740.780.8647empty

Interfaces

1 interface between chains.

  • A–B · 1341 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 5FJ5 · Structure of the in vitro assembled bacteriophage phi6 polymerase complex · the same entry in another collection · chain A against A, TM-score 1.00

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