Hyde from T. maritima in complex with S-adenosyl-L-cysteine (final product)

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 13% strand (DSSP).

Ligands and binding sites

• CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · 5 copies · chains A
• SF4 · Iron/sulfur cluster · ligand · chains A
• MET · Methionine · ligand · chains A
• 5X8 · S-adenosyl-L-cysteine · ligand · chains A
• SAH · S-adenosyl-L-homocysteine · ligand · chains A
• 41K · (2R,4R)-2-methyl-1,3-thiazolidine-2,4-dicarboxylic acid · ligand · chains A
• CL · Chloride ion · ion · 2 copies · 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.

Compared structures

• 5FEW · HydE from T. maritima in complex with S-adenosyl-L-cysteine (final product) · the same entry in another collection · chain A against A, TM-score 1.00
• Q9X0Z6 · AlphaFold monomer V2.0 prediction for [fefe] hydrogenase maturase subunit hyde (Q9X0Z6) · a predicted model of the same protein · 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 Q9X0Z6
• Elsewhere: RCSB PDB 5FEW · PDBe 5FEW · UniProt Q9X0Z6