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Crystal structure of the sifa-SKIP(PH) complex

Analyse Crystal structure of the sifa-SKIP(PH) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HW2
Type
protein
Length
413 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein sifa; Pleckstrin homology domain-containing family M member 2
UniProt
Q56061, Q8IWE5
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein sifaprotein30849% helix, 17% strandQ56061
BPleckstrin homology domain-containing family M member 2protein10514% helix, 43% strandQ8IWE5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12720.560.7734empty
21390.390.7322empty

Interfaces

1 interface between chains.

  • A–B · 727 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 3HW2 · Crystal structure of the SifA-SKIP(PH) complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q56061 · AlphaFold monomer V2.0 prediction for secreted effector protein sifa (Q56061) · a predicted model of the same protein · chain A against A, TM-score 0.95
  • Q8IWE5 · AlphaFold monomer V2.0 prediction for pleckstrin homology domain- containing family M… · a predicted model of the same protein · chain B against A, TM-score 0.91

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