GL1X · GenesisL1 explorer

Research workbench

Crystal structure of xiap-BIR2 domain

Analyse Crystal structure of xiap-BIR2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4J3Y
Type
protein
Length
160 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase xiap
EC
6.3.2.-
UniProt
P98170
Ligands
ZN
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase xiap (EC 6.3.2.-)protein8340% helix, 10% strandP98170
CE3 ubiquitin-protein ligase xiap (EC 6.3.2.-)protein7738% helix, 10% strandP98170

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, C

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
11220.440.7719empty

Interfaces

1 interface between chains.

  • A–C · 479 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 4J3Y · Crystal structure of XIAP-BIR2 domain · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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