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The structural characterization of burkholderia pseudomallei oppa.

Analyse The structural characterization of burkholderia pseudomallei oppa. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZS6
Type
protein
Length
509 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Periplasmic oligopeptide-binding protein; Oligopeptide dva
UniProt
Q63ID0
Ligands
CL
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeriplasmic oligopeptide-binding proteinprotein50635% helix, 22% strandQ63ID0
BOligopeptide dvaprotein30% helix, 33% strand—

Ligands and binding sites

  • CL · Chloride ion · ion · chains A
  • GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.750.9732empty
21790.510.7824empty
31050.360.7421empty

Interfaces

1 interface between chains.

  • A–B · 374 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3ZS6 · The Structural characterization of Burkholderia pseudomallei OppA. · the same entry in another collection · chain A against A, TM-score 1.00

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