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Cloning, sequence, and crystallographic structure of recombinant iron superoxide dismutase from pseudomonas ovalis

Analyse Cloning, sequence, and crystallographic structure of recombinant iron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DT0
Type
protein
Length
589 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase
EC
1.15.1.1
UniProt
P09223
Ligands
FE
Pockets
2 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSuperoxide dismutase (EC 1.15.1.1)protein19750% helix, 12% strandP09223
CSuperoxide dismutase (EC 1.15.1.1)protein19552% helix, 12% strandP09223

Ligands and binding sites

  • FE · Fe (III) ion · metal · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11820.550.8020empty
21920.520.7821empty

Interfaces

1 interface between chains.

  • A–B · 917 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 1DT0 · Cloning, sequence, and crystallographic structure of recombinant iron superoxide… · the same entry in another collection · chain A against A, TM-score 1.00
  • P09223 · AlphaFold monomer V2.0 prediction for superoxide dismutase [fe] (P09223) · a predicted model of the same protein · chain C against A, TM-score 0.99

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