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MolNFT v1 · #148861 · protein

Structure of fae solved by sad from data collected at the peak of the selenium absorption edge on ID30B

6FJ4 · Endo-1,4-beta-xylanase Y: “Structure of fae solved by sad from data collected at the peak of the selenium absorption edge on ID30B”. X-ray diffraction, 2 ligands (CD, SO4), 2 pockets (best druggability 0.46). MolNFT v1 #148861 on…

PDB
6FJ4
Type
protein
Length
283 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endo-1,4-beta-xylanase Y
EC
3.2.1.8
UniProt
P51584
Ligands
CD, SO4
Pockets
2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndo-1,4-beta-xylanase Y (EC 3.2.1.8)protein28333% helix, 19% strandP51584

Ligands and binding sites

  • CD · Cadmium ion · metal · 5 copies · chains A
  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1640.460.8322empty
2730.350.7613empty

Modifications

Observed in the structure: 9 modified (engineered, phosphorylation).

Compared structures

  • 6FJ4 · Structure of FAE solved by SAD from data collected at the peak of the Selenium absorption… · the same entry in another collection · chain A against A, TM-score 1.00
  • P51584 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Y (P51584) · a predicted model of the same protein · chain A against A, TM-score 0.96

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