Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SCO2 protein homolog, mitochondrial | protein | 170 | 30% helix, 23% strand | O43819 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.72 | 0.84 | 38 | empty |
| 2 | 50 | 0.60 | 0.92 | 16 | empty |
| 3 | 60 | 0.36 | 0.78 | 12 | empty |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O43819
- Elsewhere: RCSB PDB 2RLI · PDBe 2RLI · UniProt O43819
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