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Solution structure of CU(I) human SCO2

Analyse Solution structure of CU(I) human SCO2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RLI
Type
protein
Length
170 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SCO2 protein homolog, mitochondrial
UniProt
O43819
Ligands
CU1
Pockets
3 · best druggability 0.72

Structure

solution nmr · 1 distinct chain · 30% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASCO2 protein homolog, mitochondrialprotein17030% helix, 23% strandO43819

Ligands and binding sites

  • CU1 · Copper (I) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13280.720.8438empty
2500.600.9216empty
3600.360.7812empty

Compared structures

  • 2RLI · Solution structure of Cu(I) human Sco2 · the same entry in another collection · chain A against A, TM-score 1.00
  • O43819 · AlphaFold monomer V2.0 prediction for protein SCO2 homolog, mitochondrial (O43819) · a predicted model of the same protein · chain A against A, TM-score 0.80

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