MolNFT v1 · #9005 · protein

Eosinophil-derived neurotoxin (edn) - adenosine-5'-diphosphate complex

1HI5: “Eosinophil-derived neurotoxin (edn) - adenosine-5'-diphosphate complex”. X-ray diffraction, 1 ligand (ADP), 1 pocket (best druggability 0.33). MolNFT v1 #9005 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1HI5
Type: protein
Length: 135 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eosinophil-derived neurotoxin
EC: 3.1.27.5
UniProt: P10153
Ligands: ADP
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eosinophil-derived neurotoxin (EC 3.1.27.5)	protein	135	23% helix, 35% strand	P10153

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.33	0.73	26	ADP

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1HI5 · Eosinophil-derived Neurotoxin (EDN) - Adenosine-5'-Diphosphate Complex · the same entry in another collection · chain A against A, TM-score 1.00
P10153 · AlphaFold monomer V2.0 prediction for non-secretory ribonuclease (P10153) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P10153
Elsewhere: RCSB PDB 1HI5 · PDBe 1HI5 · UniProt P10153

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