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Phl P 4 N158H variant, a glucose dehydrogenase

Analyse Phl P 4 N158H variant, a glucose dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PVH
Type
protein
Length
490 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pollen allergen phl P 4.0202
UniProt
B2ZWE9
Ligands
FAD, NA
Pockets
1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APollen allergen phl P 4.0202protein49037% helix, 21% strandB2ZWE9

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • MLI · Malonate ion · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15890.820.8876FAD

Modifications

Observed in the structure: 2 cofactor, 2 disulfide (flavinylation, disulfide).

Compared structures

  • 4PVH · Phl p 4 N158H variant, a glucose dehydrogenase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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