MolNFT v1 · #153903 · protein
Aspergillus oryzae active-tyrosinase copper-bound C92A mutant complexed with L-tyrosine
6JU9: “Aspergillus oryzae active-tyrosinase copper-bound C92A mutant complexed with L-tyrosine”. X-ray diffraction, 4 ligands (TYR, DAH, CU), 10 pockets (best druggability 0.64). MolNFT v1 #153903 on GenesisL1: 3D structure, binding sites…
- PDB
- 6JU9
- Type
- protein
- Length
- 869 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosinase
- EC
- 1.14.18.1
- UniProt
- A0A1S9DK56
- Ligands
- TYR, DAH, CU, NO3
- Pockets
- 10 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase (EC 1.14.18.1) | protein | 435 | 42% helix, 11% strand | A0A1S9DK56 |
| B | Tyrosinase (EC 1.14.18.1) | protein | 434 | 42% helix, 11% strand | A0A1S9DK56 |
Ligands and binding sites
- TYR · Tyrosine · ligand · 2 copies · chains A, B
- DAH · 3,4-dihydroxyphenylalanine · ligand · chains A
- CU · Copper (II) ion · metal · 4 copies · chains A, B
- NO3 · Nitrate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.64 | 0.78 | 54 | empty |
| 2 | 529 | 0.63 | 0.76 | 60 | TYR, DAH |
| 3 | 58 | 0.47 | 0.85 | 23 | empty |
| 4 | 94 | 0.47 | 0.81 | 19 | empty |
| 5 | 94 | 0.46 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1502 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6JU9 · Aspergillus oryzae active-tyrosinase copper-bound C92A mutant complexed with L-tyrosine · 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 A0A1S9DK56
- Elsewhere: RCSB PDB 6JU9 · PDBe 6JU9 · UniProt A0A1S9DK56
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