› 3lj9

X-ray diffraction
2.1Å resolution

X-ray structure of the iron superoxide dismutase from pseudoalteromonas haloplanktis in complex with sodium azide

Released:
DOI: 10.2210/pdb3lj9/pdb
PDB entry 3lj9 coloured by chain, front view.
PDB entry 3lj9 coloured by chain, side view.
PDB entry 3lj9 coloured by chain, top view.
Source organism: Pseudoalteromonas translucida TAC125
Primary publication:
Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.
Merlino A, Russo Krauss I, Castellano I, De Vendittis E, Rossi B, Conte M, Vergara A, Sica F
J Struct Biol 172 343-52 (2010)
PMID: 20732427

Function and Biology Details

Reaction catalysed: 
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Superoxide dismutase [Fe] Chains: A, B
Molecule details ›
Chains: A, B
Length: 192 amino acids
Theoretical weight: 21.27 KDa
Source organism: Pseudoalteromonas translucida TAC125
Expression system: Escherichia coli
UniProt:
  • Canonical: P84612 (Residues: 1-192; Coverage: 100%)
Gene names: PSHAa1215, sodB
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand AZI 2 x AZI
Ligand FE 2 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 46.134Å b: 103.527Å c: 50.586Å
α: 90° β: 108.29° γ: 90°
R-values:
R R work R free
0.233 0.203 0.256
Expression system: Escherichia coli

Quick links

Citations

9 review citations

tRNA Modifications: Impact on Structure and Thermal Adaptation.
Lorenz et al. (2017)
8 more

2 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
1 more