Research workbench

Human formylglycine generating enzyme

Analyse Human formylglycine generating enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Y1E
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-alpha-formyglycine-generating enzyme
UniProt: Q8NBK3
Ligands: NAG, CA
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	C-alpha-formyglycine-generating enzyme	protein	272	16% helix, 21% strand	Q8NBK3

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains X
CA · Calcium ion · metal · 2 copies · chains X

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	153	0.50	0.78	22	empty
2	106	0.48	0.80	21	empty

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

1Y1E · human formylglycine generating enzyme · the same entry in another collection · chain X against X, TM-score 1.00
Q8NBK3 · AlphaFold monomer V2.0 prediction for formylglycine-generating enzyme (Q8NBK3) · a predicted model of the same protein · chain X 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 Q8NBK3
Elsewhere: RCSB PDB 1Y1E · PDBe 1Y1E · UniProt Q8NBK3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.