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MolNFT v1 · #4710 · protein

Study on radiation damage on a cryocooled crystal. part 1: structure prior to irradiation

1DWA · Myrosinase MA1: “Study on radiation damage on a cryocooled crystal. part 1: structure prior to irradiation”. X-ray diffraction, 7 ligands (NAG, BMA, XYP), 2 pockets (best druggability 0.73). MolNFT v1 #4710 on GenesisL1: 3D…

PDB
1DWA
Type
protein
Length
499 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myrosinase MA1
EC
3.2.1.147
UniProt
P29736
Ligands
NAG, BMA, XYP, FUC, MAN, ZN, SO4
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
MMyrosinase MA1 (EC 3.2.1.147)protein49943% helix, 18% strandP29736

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 14 copies · chains M
  • BMA · beta-D-mannopyranose · sugar · 2 copies
  • XYP · beta-D-xylopyranose · sugar · 2 copies
  • FUC · alpha-L-fucopyranose · sugar · 2 copies · chains M
  • MAN · alpha-D-mannopyranose · sugar · 2 copies · chains M
  • ZN · Zinc ion · metal · chains M
  • SO4 · Sulfate ion · ion · 8 copies · chains M
  • GOL · Glycerol · additive · 5 copies · chains M

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15770.730.8051SO4, GOL
21350.400.7423empty

Modifications

Observed in the structure: 10 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

  • 1DWA · Study on radiation damage on a cryocooled crystal. part 1: structure prior to irradiation · the same entry in another collection · chain M against M, TM-score 1.00
  • P29736 · AlphaFold monomer V2.0 prediction for myrosinase MA1 (P29736) · a predicted model of the same protein · chain M against A, TM-score 1.00

Analyse

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