› 5kh0

X-ray diffraction
2.8Å resolution

Crystal Structure of HydF from thermosipho melanesiensis in complex with a [4Fe-4S] cluster

Released:
DOI: 10.2210/pdb5kh0/pdb
PDB 5kh0 coloured by chain and viewed from the front.
PDB 5kh0 coloured by chain and viewed from the side.
PDB 5kh0 coloured by chain and viewed from the top.
Source organism: Thermosipho melanesiensis BI429
Primary publication:
Structural and functional characterization of the hydrogenase-maturation HydF protein.
Caserta G, Pecqueur L, Adamska-Venkatesh A, Papini C, Roy S, Artero V, Atta M, Reijerse E, Lubitz W, Fontecave M
Nat Chem Biol 13 779-784 (2017)
PMID: 28553946

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small GTP-binding protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 396 amino acids
Theoretical weight: 44.35 KDa
Source organism: Thermosipho melanesiensis BI429
Expression system: Escherichia coli
UniProt:
  • Canonical: A6LMQ7 (Residues: 1-396; Coverage: 100%)
Gene name: Tmel_1361
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SF4 4 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 72.01Å b: 173.48Å c: 89.32Å
α: 90° β: 110.01° γ: 90°
R-values:
R R work R free
0.234 0.233 0.262
Expression system: Escherichia coli

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Citations

3 review citations

Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.
Britt et al. (2020)
2 more