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Crystal structure of the N-terminal regulatory domains of the formin FHOD1

Analyse Crystal structure of the N-terminal regulatory domains of the formin FHOD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DAD
Type
protein
Length
635 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
FH1/FH2 domain-containing protein 1
UniProt
Q9Y613
Pockets
6 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFH1/FH2 domain-containing protein 1protein32461% helix, 8% strandQ9Y613
BFH1/FH2 domain-containing protein 1protein31161% helix, 5% strandQ9Y613

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12600.560.7729empty
21280.500.8019empty
31130.490.8018empty
41280.490.7916empty
51320.470.7819empty

Interfaces

1 interface between chains.

  • A–B · 562 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 3DAD · Crystal structure of the N-terminal regulatory domains of the formin FHOD1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y613 · AlphaFold monomer V2.0 prediction for FH1/FH2 domain-containing protein 1 (Q9Y613) · a predicted model of the same protein · chain B against A, TM-score 0.98

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