MolNFT v1 · #118878 · protein
Copm in the CU(II)-bound form
5FFC: “Copm in the CU(II)-bound form”. X-ray diffraction, 2 ligands (CU, SO4), 1 pocket (best druggability 0.64). MolNFT v1 #118878 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FFC
- Type
- protein
- Length
- 281 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copm
- UniProt
- A0A0F6QDN6
- Ligands
- CU, SO4
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copm | protein | 148 | 77% helix, 0% strand | A0A0F6QDN6 |
| B | Copm | protein | 133 | 86% helix, 0% strand | A0A0F6QDN6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.64 | 0.76 | 46 | empty |
Interfaces
1 interface between chains.
- A–B · 404 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5FFC · CopM in the Cu(II)-bound form · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0F6QDN6
- Elsewhere: RCSB PDB 5FFC · PDBe 5FFC · UniProt A0A0F6QDN6
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