› 5few

X-ray diffraction
1.17Å resolution

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

Released:
DOI: 10.2210/pdb5few/pdb
PDB entry 5few coloured by chain, front view.
PDB entry 5few coloured by chain, side view.
PDB entry 5few coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.
Rohac R, Amara P, Benjdia A, Martin L, Ruffié P, Favier A, Berteau O, Mouesca JM, Fontecilla-Camps JC, Nicolet Y
Nat Chem 8 491-500 (2016)
PMID: 27102684

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[FeFe] hydrogenase maturase subunit HydE Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 41.01 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0Z6 (Residues: 2-348; Coverage: 100%)
Gene names: THEMA_07990, TM_1269, Tmari_1274
Sequence domains: Radical SAM superfamily
Structure domains: Aldolase class I

Ligands and Environments

7 bound ligands:
Ligand SF4 1 x SF4
Ligand CPS 5 x CPS
Ligand CL 2 x CL
Ligand MET 1 x MET
Ligand 5X8 1 x 5X8
Ligand SAH 1 x SAH
Ligand 41K 1 x 41K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 50.99Å b: 78.97Å c: 86.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.111 0.11 0.132
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides (RiPPs).
Benjdia et al. (2017)
10 more

1 mention without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)