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Crystal structure of the virion-associated protein P3 from caulimovirus

Analyse Crystal structure of the virion-associated protein P3 from caulimovirus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3K4T
Type
protein
Length
282 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Virion-associated protein
UniProt
P03551
Ligands
CL
Pockets
2 · best druggability 0.84

Structure

x-ray diffraction · 4 distinct chains · 83% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVirion-associated proteinprotein7086% helix, 0% strandP03551
BVirion-associated proteinprotein7183% helix, 0% strandP03551
CVirion-associated proteinprotein7377% helix, 0% strandP03551
DVirion-associated proteinprotein6885% helix, 0% strandP03551

Ligands and binding sites

  • CL · Chloride ion · ion · chains B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11870.840.9826empty
21390.630.8622CL

Interfaces

6 interfaces between chains.

  • A–C · 1714 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 1674 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 1631 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 1561 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 274 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 3K4T · Crystal structure of the virion-associated protein P3 from caulimovirus · the same entry in another collection · chain A against A, TM-score 1.00

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