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Superoxide dismutase from sulfolobus acidocaldarius

Analyse Superoxide dismutase from sulfolobus acidocaldarius in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1B06
Type
protein
Length
1,248 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (superoxide dismutase)
EC
1.15.1.1
UniProt
Q08713
Ligands
FE
Pockets
10 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FProtein (superoxide dismutase) (EC 1.15.1.1)protein20851% helix, 11% strandQ08713

Ligands and binding sites

  • FE · Fe (III) ion · metal · 6 copies · chains A, B, C, D, E, F

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

Pockets

10 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110010.730.7681empty
211530.720.7689empty
34260.630.7743empty
44570.630.7740empty
53610.600.7639empty

Interfaces

11 interfaces between chains.

  • C–E · 2416 Ų buried · 38 hydrogen bonds · protein-protein
  • D–F · 2409 Ų buried · 39 hydrogen bonds · protein-protein
  • A–B · 915 Ų buried · 19 hydrogen bonds · protein-protein
  • E–F · 906 Ų buried · 16 hydrogen bonds · protein-protein
  • C–D · 904 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 1B06 · Superoxide dismutase from sulfolobus acidocaldarius · the same entry in another collection · chain C against C, TM-score 1.00
  • Q08713 · AlphaFold monomer V2.0 prediction for superoxide dismutase [fe] (Q08713) · a predicted model of the same protein · chain A against A, TM-score 1.00

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