MolNFT v1 · #33093 · protein
CU(I)CU(II)-copc at pH 4.5
2C9P · Copper resistance protein C: “CU(I)CU(II)-copc at pH 4.5”. X-ray diffraction, 2 ligands (CU, NO3), 3 pockets (best druggability 0.44). MolNFT v1 #33093 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2C9P
- Type
- protein
- Length
- 306 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper resistance protein C
- UniProt
- P12376
- Ligands
- CU, NO3
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Copper resistance protein C | protein | 102 | 0% helix, 52% strand | P12376 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 6 copies · chains A, B, C
- NO3 · Nitrate ion · ion · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.44 | 0.77 | 25 | empty |
| 2 | 61 | 0.37 | 0.79 | 27 | empty |
| 3 | 51 | 0.30 | 0.76 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–B · 598 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 228 Ų buried · 1 hydrogen bond · protein-protein
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 P12376
- Elsewhere: RCSB PDB 2C9P · PDBe 2C9P · UniProt P12376
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