› 1eso

X-ray diffraction
2Å resolution

MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1eso/pdb
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PDB entry 1eso coloured by chain, front view.
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PDB entry 1eso coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography.
Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, Bolognesi M
J Mol Biol 274 408-20 (1997)
PMID: 9405149

Function and Biology Details

Reaction catalysed: 
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142804 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 15.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGD1 (Residues: 20-173; Coverage: 100%)
Gene names: JW1638, b1646, sodC
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand CU 1 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 33Å b: 52.4Å c: 43.2Å
α: 90° β: 111.2° γ: 90°
R-values:
R R work R free
0.168 0.168 0.26
Expression system: Escherichia coli

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Citations

8 review citations

Superoxide dismutases and superoxide reductases.
Sheng et al. (2014)
7 more

11 mentions without citation

A Short Tale of the Origin of Proteins and Ribosome Evolution.
Farías-Rico et al. (2022)
10 more

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