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Crystal structure of the human FE65-PTB1 domain

Analyse Crystal structure of the human FE65-PTB1 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3D8D
Type
protein
Length
278 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amyloid beta A4 precursor protein-binding family B member 1
UniProt
O00213
Ligands
HG
Pockets
4 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAmyloid beta A4 precursor protein-binding family B member 1protein13926% helix, 35% strandO00213

Ligands and binding sites

  • HG · Mercury (II) ion · metal · 6 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12660.580.7839empty
22310.520.7630HG
31180.420.7723empty
4990.400.7722empty

Interfaces

1 interface between chains.

  • A–B · 339 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3D8D · Crystal structure of the human Fe65-PTB1 domain · the same entry in another collection · chain A against A, TM-score 1.00
  • O00213 · AlphaFold monomer V2.0 prediction for amyloid-beta A4 precursor protein-binding family B… · a predicted model of the same protein · chain B against A, TM-score 0.99

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