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Crystal structure of phaeospaeria nodrum fructosyl peptide oxidase

Analyse Crystal structure of phaeospaeria nodrum fructosyl peptide oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T1E
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q0UIL6
Ligands: FAD
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	431	31% helix, 26% strand	Q0UIL6

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
ACY · Acetic acid · additive · 3 copies · chains A

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

Pockets

5 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	1016	0.82	0.83	98	FAD, ACY
2	53	0.70	0.97	18	empty
3	57	0.44	0.83	20	empty
4	68	0.42	0.81	19	empty
5	50	0.25	0.72	18	empty

Modifications

Observed in the structure: 1 cofactor (flavinylation).

Compared structures

5T1E · Crystal structure of Phaeospaeria nodrum fructosyl peptide oxidase · 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 Q0UIL6
Elsewhere: RCSB PDB 5T1E · PDBe 5T1E · UniProt Q0UIL6

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