› 5ff2

X-ray diffraction
1.47Å resolution

HydE from T. maritima in complex with (2R,4R)-TDA

Released:
DOI: 10.2210/pdb5ff2/pdb
PDB entry 5ff2 coloured by chain, front view.
PDB entry 5ff2 coloured by chain, side view.
PDB entry 5ff2 coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
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: 348 amino acids
Theoretical weight: 39.86 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0Z6 (Residues: 1-348; Coverage: 100%)
Gene names: THEMA_07990, TM_1269, Tmari_1274
Sequence domains: Radical SAM superfamily
Structure domains: Aldolase class I

Ligands and Environments

6 bound ligands:
Ligand SF4 1 x SF4
Ligand CPS 5 x CPS
Ligand CL 1 x CL
Ligand SAH 1 x SAH
Ligand 5XB 1 x 5XB
Ligand H2S 2 x H2S
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 51.23Å b: 79.09Å c: 86.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.187
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

Protection of abasic sites during DNA replication by a stable thiazolidine protein-DNA cross-link.
Thompson et al. (2019)