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Structure of the C-terminal domain of EHD1 with fnyestgpftak

Analyse Structure of the C-terminal domain of EHD1 with fnyestgpftak in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KFH
Type
protein
Length
117 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Eh domain-containing protein 1; RAB11-FIP2 gpf peptide fnyestgpftak
UniProt
Q9H4M9
Ligands
CA
Pockets
1 · best druggability 0.38

Structure

solution nmr · 2 distinct chains · 40% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEh domain-containing protein 1protein10545% helix, 5% strandQ9H4M9
BRAB11-FIP2 gpf peptide fnyestgpftakprotein120% helix, 0% strand—

Ligands and binding sites

  • CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1640.380.7817empty

Interfaces

1 interface between chains.

  • A–B · 276 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 2KFH · Structure of the C-terminal domain of EHD1 with FNYESTGPFTAK · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H4M9 · AlphaFold monomer V2.0 prediction for eh domain-containing protein 1 (Q9H4M9) · a predicted model of the same protein · chain A against A, TM-score 0.83

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