MolNFT v1 · #27107 · protein
Umecyanin from horse raddish- crystal structure of the oxidised form
1X9R: “Umecyanin from horse raddish- crystal structure of the oxidised form”. X-ray diffraction, 1 ligand (CU), 2 pockets (best druggability 0.58). MolNFT v1 #27107 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1X9R
- Type
- protein
- Length
- 209 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Umecyanin
- UniProt
- P42849
- Ligands
- CU
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Umecyanin | protein | 105 | 13% helix, 31% strand | P42849 |
| B | Umecyanin | protein | 104 | 13% helix, 31% strand | P42849 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.58 | 0.87 | 28 | empty |
| 2 | 51 | 0.39 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 564 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P42849
- Elsewhere: RCSB PDB 1X9R · PDBe 1X9R · UniProt P42849
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.