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Human formylglycine generating enzyme, oxidised cys refined as hydroperoxide

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

PDB: 1Y1H
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-alpha-formyglycine-generating enzyme
Ligands: PEO, NAG, SR
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	C-alpha-formyglycine-generating enzyme	protein	275	16% helix, 22% strand	—

Ligands and binding sites

PEO · Hydrogen peroxide · ligand · chains X
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains X
SR · Strontium 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	181	0.55	0.79	23	PEO
2	109	0.48	0.80	20	empty

Modifications

Observed in the structure: 2 disulfide, 1 covalent, 1 glycan (disulfide, covalent ligand, N-glycosylation).

Compared structures

1Y1H · human formylglycine generating enzyme, oxidised Cys refined as hydroperoxide · the same entry in another collection · chain X against X, 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 1Y1H · PDBe 1Y1H

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