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Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfl

Analyse Structure of the second EPS15 homology domain of human EPS15 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FF1
Type
protein
Length
101 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Epidermal growth factor receptor substrate 15; Ptgssstnpfl peptide
UniProt
P42566
Ligands
CA
Pockets
1 · best druggability 0.31

Structure

solution nmr · 2 distinct chains · 48% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEpidermal growth factor receptor substrate 15protein9551% helix, 2% strandP42566
BPtgssstnpfl peptideprotein60% 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
1500.310.7616empty

Interfaces

1 interface between chains.

  • A–B · 353 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1FF1 · Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfl · the same entry in another collection · chain A against A, TM-score 1.00
  • P42566 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor substrate 15… · a predicted model of the same protein · chain A against A, TM-score 0.90

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