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Crystal structure of a fimbrial biogenesis protein PILY2 (PILY2_PA4555) from pseudomonas aeruginosa PAO1 at 2.10 a resolution

Analyse Crystal structure of a fimbrial biogenesis protein PILY2 (PILY2_PA4555) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TDQ
Type
protein
Length
163 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PILY2 protein
UniProt
Q51537
Ligands
NA, CL
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APILY2 proteinprotein8616% helix, 47% strandQ51537
BPILY2 proteinprotein7718% helix, 49% strandQ51537

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • CL · Chloride ion · ion · chains A, B
  • GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.360.7913GOL

Interfaces

1 interface between chains.

  • A–B · 923 Ų buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 3TDQ · Crystal structure of a fimbrial biogenesis protein PilY2 (PilY2_PA4555) from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00

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