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Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 ångströms resolution

Analyse Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SXB
Type
protein
Length
302 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase
EC
1.15.1.1
UniProt
P00442
Ligands
CU, ZN
Pockets
2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSuperoxide dismutase (EC 1.15.1.1)protein1515% helix, 42% strandP00442

Ligands and binding sites

  • CU · Copper (II) ion · metal · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B

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
11750.630.8534empty
2860.340.7517empty

Interfaces

1 interface between chains.

  • A–B · 724 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1SXB · Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00442 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P00442) · a predicted model of the same protein · chain A against A, TM-score 1.00

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