MolNFT v1 · #142522 · protein

Crystal structure of the modified fructosyl peptide oxidase from aspergillus nidulans with R61G mutation

6A6T · Fructosyl amine: oxygen oxidoreductase: “Crystal structure of the modified fructosyl peptide oxidase from aspergillus nidulans with R61G mutation”. X-ray diffraction, 3 ligands (D1D, FAD, SO4), 2 pockets (best druggability 0.83).…

PDB: 6A6T
Type: protein
Length: 430 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructosyl amine: oxygen oxidoreductase
Ligands: D1D, FAD, SO4
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructosyl amine: oxygen oxidoreductase	protein	430	30% helix, 26% strand	—

Ligands and binding sites

D1D · (4S,5S)-1,2-dithiane-4,5-diol · ligand · 5 copies · chains A
FAD · Flavin-adenine dinucleotide · ligand · chains A
SO4 · Sulfate ion · ion · 4 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1038	0.83	0.84	109	FAD, D1D
2	155	0.52	0.79	27	SO4

Modifications

Observed in the structure: 1 cofactor, 1 modified (flavinylation, oxidation).

Compared structures

6A6T · Crystal structure of the modified fructosyl peptide oxidase from Aspergillus nidulans… · 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
Elsewhere: RCSB PDB 6A6T · PDBe 6A6T

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