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1.24 ångströms resolution structure of zn-zn human superoxide dismutase

Analyse 1.24 ångströms resolution structure of zn-zn human superoxide dismutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C9S
Type
protein
Length
306 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase [cu-zn]
EC
1.15.1.1
UniProt
P00441
Ligands
ZN, SO4
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, FSuperoxide dismutase [cu-zn] (EC 1.15.1.1)protein1535% helix, 41% strandP00441

Ligands and binding sites

  • ZN · Zinc ion · metal · 6 copies · chains A, F
  • SO4 · Sulfate ion · ion · 6 copies · chains A, F
  • ACT · Acetate ion · additive · 3 copies · chains A, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.570.8131empty
2940.320.7324empty

Interfaces

1 interface between chains.

  • A–F · 696 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 2 modified (disulfide, oxidation).

Compared structures

  • 2C9S · 1.24 Angstroms resolution structure of Zn-Zn Human Superoxide dismutase · the same entry in another collection · chain A against A, TM-score 1.00

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