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Crystal structure of the type III secretion chaperone syct from yersinia enterocolitica (crystal form 2)

Analyse Crystal structure of the type III secretion chaperone syct from yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BSH
Type
protein
Length
236 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Syct
UniProt
O85243
Pockets
2 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASyctprotein12026% helix, 31% strandO85243
BSyctprotein11632% helix, 31% strandO85243

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11190.470.8021empty
2720.350.7716empty

Interfaces

1 interface between chains.

  • A–B · 1106 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 2BSH · Crystal structure of the type III secretion chaperone SycT from Yersinia enterocolitica… · the same entry in another collection · chain A against A, TM-score 1.00

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