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Crystal structure of bacteriophage CBA120 tailspike protein 3 (TSP3, ORF212)

Analyse Crystal structure of bacteriophage CBA120 tailspike protein 3 (TSP3, ORF212) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5W6F
Type
protein
Length
1,848 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tailspike protein 3
UniProt
G3M191
Ligands
CL
Pockets
19 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CTailspike protein 3protein61611% helix, 43% strandG3M191

Ligands and binding sites

  • CL · Chloride ion · ion · chains A, C

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

Pockets

19 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110980.850.8679empty
211460.840.85100empty
3620.751.0015empty
4740.730.9815empty
5820.730.9721empty

Interfaces

3 interfaces between chains.

  • B–C · 4889 Ų buried · 72 hydrogen bonds · protein-protein
  • A–C · 4885 Ų buried · 75 hydrogen bonds · protein-protein
  • A–B · 4877 Ų buried · 71 hydrogen bonds · protein-protein

Compared structures

  • 5W6F · Crystal structure of Bacteriophage CBA120 tailspike protein 3 (TSP3, orf212) · the same entry in another collection · chain A against A, TM-score 1.00

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