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Structure of SYE1, an oye homologue from S. oneidensis, in complex with P-hydroxybenzaldehyde

Analyse Structure of SYE1, an oye homologue from S. oneidensis, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GQ9
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxidoreductase, FMN-binding
UniProt: Q8EEC8
Ligands: HBA, FMN, SO4
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxidoreductase, FMN-binding	protein	362	36% helix, 17% strand	Q8EEC8

Ligands and binding sites

HBA · P-hydroxybenzaldehyde · ligand · 2 copies · chains A
FMN · Flavin mononucleotide · ligand · chains A
SO4 · Sulfate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	425	0.78	0.86	48	FMN, HBA
2	68	0.29	0.73	17	empty

Compared structures

2GQ9 · Structure of SYE1, an OYE homologue from S. oneidensis, in complex with… · 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 Q8EEC8
Elsewhere: RCSB PDB 2GQ9 · PDBe 2GQ9 · UniProt Q8EEC8

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