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Crystal structure of the human spir-1 kind fsi domain in complex with the fsi peptide

Analyse Crystal structure of the human spir-1 kind fsi domain in complex with the fsi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YLE
Type
protein
Length
192 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein spire homolog 1; Formin-2
UniProt
Q08AE8, Q9NZ56
Pockets
2 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein spire homolog 1protein17153% helix, 8% strandQ08AE8
BFormin-2protein2129% helix, 14% strandQ9NZ56

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.380.8015empty
2710.320.7421empty

Interfaces

1 interface between chains.

  • A–B · 1044 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 2YLE · Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q08AE8 · AlphaFold monomer V2.0 prediction for protein spire homolog 1 (Q08AE8) · a predicted model of the same protein · chain A against A, TM-score 0.94
  • Q9NZ56 · AlphaFold monomer V2.0 prediction for formin-2 (Q9NZ56) · a predicted model of the same protein · chain B against A, TM-score 0.31

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