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MolNFT v1 · #4343 · protein

Crystal structure of class I alpha-1,2-mannosidase from saccharomyces cerevisiae at 1.54 ångström resolution

1DL2: “Crystal structure of class I alpha-1,2-mannosidase from saccharomyces cerevisiae at 1.54 ångström resolution”. X-ray diffraction, 5 ligands (NAG, MAN, BMA), 3 pockets (best druggability 0.63). MolNFT v1 #4343 on GenesisL1: 3D…

PDB
1DL2
Type
protein
Length
510 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Class I alpha-1,2-mannosidase
EC
3.2.1.113
UniProt
P32906
Ligands
NAG, MAN, BMA, NDG, CA
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AClass I alpha-1,2-mannosidase (EC 3.2.1.113)protein51050% helix, 11% strandP32906

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · 2 copies
  • NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
  • CA · Calcium ion · metal · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12790.630.8145CA, GOL
2590.470.8419empty
31170.440.7719NAG

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1DL2 · Crystal structure of class I alpha-1,2-mannosidase from saccharomyces cerevisiae at 1.54… · the same entry in another collection · chain A against A, TM-score 1.00
  • P32906 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum mannosyl- oligosaccharide… · a predicted model of the same protein · chain A against A, TM-score 1.00

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