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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 v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.4
Source: Phleum pratense
Molecule: Pollen allergen Phl p 4.0202
UniProt: B2ZWE9
Ligands: FAD, NA
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · resolution 1.4 · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pollen allergen Phl p 4.0202	protein	490	37% helix, 21% strand	B2ZWE9

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	589	0.82	0.88	76	FAD

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

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B2ZWE9
Elsewhere: RCSB PDB 4PVH · PDBe 4PVH · UniProt B2ZWE9

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