› 6s3x

X-ray diffraction
1.72Å resolution

Crystal Structure of the Homospermidine Synthase (HSS) variant E210Q from Blastochloris viridis in Complex with NAD

Released:
DOI: 10.2210/pdb6s3x/pdb
PDB entry 6s3x coloured by chain, front view.
PDB entry 6s3x coloured by chain, side view.
PDB entry 6s3x coloured by chain, top view.
Source organism: Blastochloris viridis
Primary publication:
Structural and catalytic characterization of Blastochloris viridis and Pseudomonas aeruginosa homospermidine synthases supports the essential role of cation-π interaction.
Helfrich F, Scheidig AJ
Acta Crystallogr D Struct Biol 77 1317-1335 (2021)
PMID: 34605434

Function and Biology Details

Reaction catalysed: 
2 putrescine = sym-homospermidine + NH(3)
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-128445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homospermidine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 480 amino acids
Theoretical weight: 53.04 KDa
Source organism: Blastochloris viridis
Expression system: Escherichia coli
UniProt:
  • Canonical: O32323 (Residues: 2-477; Coverage: 100%)
Gene name: hss
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand SO4 2 x SO4
Ligand AG2 2 x AG2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Unit cell:
a: 60.325Å b: 110.1Å c: 158.153Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.195
Expression system: Escherichia coli

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Citations

1 mention without citation

Structural and catalytic characterization of Blastochloris viridis and Pseudomonas aeruginosa homospermidine synthases supports the essential role of cation-π interaction.
Helfrich et al. (2021)