› 4ntd

X-ray diffraction
1.6Å resolution

Crystal structure of HlmI

Released:
DOI: 10.2210/pdb4ntd/pdb
PDB entry 4ntd coloured by chain, front view.
PDB entry 4ntd coloured by chain, side view.
PDB entry 4ntd coloured by chain, top view.
Source organism: Streptomyces clavuligerus
Primary publication:
Flavoenzyme-catalyzed formation of disulfide bonds in natural products.
Scharf DH, Groll M, Habel A, Heinekamp T, Hertweck C, Brakhage AA, Huber EM
Angew Chem Int Ed Engl 53 2221-4 (2014)
PMID: 24446392

Function and Biology Details

Reaction catalysed: 
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122842 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD/NAD(P)-binding domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 35.99 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli
UniProt:
  • Canonical: E2PZ87 (Residues: 30-354; Coverage: 92%)
Gene name: SCLAV_5275
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
4 bound ligands:
Ligand GSH 1 x GSH
Ligand GOL 1 x GOL
Ligand CL 1 x CL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3121
Unit cell:
a: 96.35Å b: 96.35Å c: 133.49Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.146 0.159
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Oxidative Cyclization in Natural Product Biosynthesis.
Tang et al. (2017)
3 more

1 mention without citation

Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase.
Buey et al. (2017)