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Crystal structure of yeast FAD synthetase (FAD1) in complex with FAD

Analyse Crystal structure of yeast FAD synthetase (FAD1) in complex with FAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WSI
Type: protein
Length: 285 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD synthetase
EC: 2.7.7.2
UniProt: P38913
Ligands: FAD, SO4
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD synthetase (EC 2.7.7.2)	protein	285	43% helix, 10% strand	P38913

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · 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

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	513	0.72	0.81	41	SO4, FAD

Compared structures

2WSI · Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD · the same entry in another collection · chain A against A, TM-score 1.00
P38913 · AlphaFold monomer V2.0 prediction for FAD synthase (P38913) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P38913
Elsewhere: RCSB PDB 2WSI · PDBe 2WSI · UniProt P38913

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