GL1X · GenesisL1 explorer

Research workbench

The Crystal Structure of Apaf from Biortus.

Analyse The Crystal Structure of Apaf from Biortus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8XQK
Type
protein
Length
381 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.85
Source
Homo sapiens
Molecule
Apoptotic protease-activating factor 1
UniProt
O14727
Ligands
PO4
Pockets
4 · best druggability 0.52

Structure

x-ray diffraction · resolution 2.85 · 3 distinct chains · 70% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DApoptotic protease-activating factor 1protein9374% helix, 0% strandO14727
BApoptotic protease-activating factor 1protein9867% helix, 0% strandO14727
CApoptotic protease-activating factor 1protein9770% helix, 0% strandO14727

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 5 copies · chains A, B, C, D

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
12440.520.7627empty
22410.510.7530empty
3770.370.7719empty
4590.370.7917empty

Interfaces

3 interfaces between chains.

  • A–B · 548 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 451 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 226 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • O14727 · AlphaFold monomer V2.0 prediction for apoptotic protease-activating factor 1 (O14727) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.