GL1X · GenesisL1 explorer

MolNFT v1 · #125678 · protein

Structure of the deglycosylated porcine aminopeptidase N ectodomain

5LG6: “Structure of the deglycosylated porcine aminopeptidase N ectodomain”. X-ray diffraction, 2 ligands (NAG, ZN), 13 pockets (best druggability 0.82). MolNFT v1 #125678 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5LG6
Type
protein
Length
1,776 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminopeptidase N
EC
3.4.11.2
UniProt
P15145
Ligands
NAG, ZN
Pockets
13 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAminopeptidase N (EC 3.4.11.2)protein88947% helix, 20% strandP15145
BAminopeptidase N (EC 3.4.11.2)protein88747% helix, 20% strandP15145

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 18 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111740.820.83112ZN
211450.810.82105ZN
33450.690.8333empty
43380.680.8233empty
54200.660.7950empty

Interfaces

1 interface between chains.

  • A–B · 410 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 48 modified, 18 glycan, 4 disulfide (engineered, N-glycosylation, disulfide).

Compared structures

  • 5LG6 · Structure of the deglycosylated porcine aminopeptidase N ectodomain · the same entry in another collection · chain A against A, TM-score 1.00
  • P15145 · AlphaFold monomer V2.0 prediction for aminopeptidase N (P15145) · a predicted model of the same protein · chain B against A, TM-score 0.99

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