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Golgi alpha-mannosidase II complex with benzyl-mannostatin a

Analyse Golgi alpha-mannosidase II complex with benzyl-mannostatin a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2F7P
Type
protein
Length
1,014 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-mannosidase II
EC
3.2.1.114
UniProt
Q24451
Ligands
2SK, NAG, ZN
Pockets
12 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-mannosidase II (EC 3.2.1.114)protein101424% helix, 30% strandQ24451

Ligands and binding sites

  • 2SK · (1R,2R,3R,4S,5R)-4-(benzylamino)-5-(methylthio)cyclopentane-1,2,3-triol · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • ZN · Zinc ion · metal · chains A
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11400.800.9734empty
22560.740.8839empty
36160.710.7989empty
42630.630.8134empty
52370.530.76352SK

Modifications

Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 2F7P · Golgi alpha-mannosidase II complex with benzyl-mannostatin A · the same entry in another collection · chain A against A, TM-score 1.00
  • Q24451 · AlphaFold monomer V2.0 prediction for alpha-mannosidase 2 (Q24451) · a predicted model of the same protein · chain A against A, TM-score 1.00

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