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Crystal structure of human SCO1 complexed with nickel.

Analyse Crystal structure of human SCO1 complexed with nickel. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GGT
Type
protein
Length
327 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SCO1 protein homolog, mitochondrial
UniProt
O75880
Ligands
NI, CL
Pockets
3 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASCO1 protein homolog, mitochondrialprotein16434% helix, 29% strandO75880
BSCO1 protein homolog, mitochondrialprotein16331% helix, 23% strandO75880

Ligands and binding sites

  • NI · Nickel (II) ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B

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
12920.670.8237NI, CL
21510.500.7822empty
3800.340.7522CL

Interfaces

1 interface between chains.

  • A–B · 659 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2GGT · Crystal structure of human SCO1 complexed with nickel. · the same entry in another collection · chain A against A, TM-score 1.00
  • O75880 · AlphaFold monomer V2.0 prediction for protein SCO1 homolog, mitochondrial (O75880) · a predicted model of the same protein · chain A against A, TM-score 0.98

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