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Golgi alpha-mannosidase II in complex with mannostatin analog (1R,2R, 3R,4S,5R)-4-amino-5-methoxycyclopentane-1,2,3-triol

Analyse Golgi alpha-mannosidase II in complex with mannostatin analog (1R,2R… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DX4
Type
protein
Length
1,016 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-mannosidase 2
EC
3.2.1.114
UniProt
Q24451
Ligands
GOO, NAG, ZN
Pockets
13 · best druggability 0.80

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-mannosidase 2 (EC 3.2.1.114)protein101624% helix, 30% strandQ24451

Ligands and binding sites

  • GOO · (1R,2R,3R,4S,5R)-4-amino-5-methoxycyclopentane-1,2,3-triol · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • ZN · Zinc ion · metal · chains A
  • MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A

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

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.800.9829empty
21670.760.9330empty
36520.720.7992empty
42570.620.8132empty
52370.540.7734GOO

Modifications

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

Compared structures

  • 3DX4 · Golgi alpha-Mannosidase II in complex with Mannostatin analog… · the same entry in another collection · chain A against A, TM-score 1.00

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