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Crystal structure of spire kind domain in complex with the tail of FMN2

Analyse Crystal structure of spire kind domain in complex with the tail of FMN2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3R7G
Type
protein
Length
173 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
1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein spire homolog 1protein15457% helix, 8% strandQ08AE8
BFormin-2protein1932% helix, 16% strandQ9NZ56

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.370.8016empty

Interfaces

1 interface between chains.

  • A–B · 925 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 3R7G · Crystal structure of Spire KIND domain in complex with the tail of FMN2 · 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 0.99
  • Q9NZ56 · AlphaFold monomer V2.0 prediction for formin-2 (Q9NZ56) · a predicted model of the same protein · chain B against A, TM-score 0.40

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