GL1X · GenesisL1 explorer

MolNFT v1 · #14246 · protein

Aminopeptidase P from escherichia COLI

1M35: “Aminopeptidase P from escherichia COLI”. X-ray diffraction, 1 ligand (MN), 20 pockets (best druggability 0.86). MolNFT v1 #14246 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
1M35
Type
protein
Length
2,640 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminopeptidase P
EC
3.4.11.9
UniProt
P15034
Ligands
MN
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FAminopeptidase P (EC 3.4.11.9)protein44041% helix, 19% strandP15034

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 12 copies · chains A, B, C, D, E, F

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

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19230.860.8896MN
23060.830.9443empty
311900.820.83107MN
411560.810.83113MN
510360.810.83103empty

Interfaces

7 interfaces between chains.

  • A–D · 2207 Ų buried · 45 hydrogen bonds · protein-protein
  • B–C · 2203 Ų buried · 48 hydrogen bonds · protein-protein
  • C–D · 687 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 684 Ų buried · 10 hydrogen bonds · protein-protein
  • E–F · 662 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 1M35 · Aminopeptidase P from Escherichia coli · the same entry in another collection · chain F against F, TM-score 1.00
  • P15034 · AlphaFold monomer V2.0 prediction for xaa-pro aminopeptidase (P15034) · a predicted model of the same protein · chain A against A, TM-score 1.00

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