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Structure of the two C-terminal domains of bacteriophage K GP144

Analyse Structure of the two C-terminal domains of bacteriophage K GP144 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5M9F
Type
protein
Length
634 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ORF68
UniProt
Q6Y7P9
Ligands
NA
Pockets
8 · best druggability 0.89

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BORF68protein2128% helix, 53% strandQ6Y7P9
CORF68protein21010% helix, 54% strandQ6Y7P9

Ligands and binding sites

  • NA · Sodium ion · metal · chains A, B, C
  • ACT · Acetate ion · additive · 5 copies · chains A, C, B

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14340.890.9755ACT
22200.630.8335empty
3860.380.7722empty
4900.380.7622empty
5500.340.7913empty

Interfaces

3 interfaces between chains.

  • A–B · 1667 Ų buried · 24 hydrogen bonds · protein-protein
  • A–C · 1646 Ų buried · 27 hydrogen bonds · protein-protein
  • B–C · 1539 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 5M9F · Structure of the two C-terminal domains of bacteriophage K gp144 · the same entry in another collection · chain A against A, TM-score 1.00

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