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Neurolysin (endopeptidase 24.16) crystal structure

Analyse Neurolysin (endopeptidase 24.16) crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1I1I
Type
protein
Length
665 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Neurolysin
EC
3.4.24.16
UniProt
P42676
Ligands
ZN
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
PNeurolysin (EC 3.4.24.16)protein66559% helix, 7% strandP42676

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains P

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110320.750.7788empty
28350.740.7983empty
3690.420.8118empty

Compared structures

  • 1I1I · Neurolysin (endopeptidase 24.16) crystal structure · the same entry in another collection · chain P against P, TM-score 1.00
  • P42676 · AlphaFold monomer V2.0 prediction for neurolysin, mitochondrial (P42676) · a predicted model of the same protein · chain P against A, TM-score 0.97

Analyse

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