Research workbench
Aspergillus oryzae active-tyrosinase copper-depleted C92A mutant complexed with L-tyrosine
Analyse Aspergillus oryzae active-tyrosinase copper-depleted C92A mutant complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JU7
- Type
- protein
- Length
- 875 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.42
- Source
- Aspergillus oryzae
- Molecule
- Tyrosinase
- EC
- 1.14.18.1
- UniProt
- A0A1S9DK56
- Ligands
- TYR, NO3
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · resolution 1.42 · 2 distinct chains · 41% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase (EC 1.14.18.1) | protein | 437 | 40% helix, 11% strand | A0A1S9DK56 |
| B | Tyrosinase (EC 1.14.18.1) | protein | 438 | 41% helix, 11% strand | A0A1S9DK56 |
Ligands and binding sites
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 | 439 | 0.65 | 0.78 | 54 | empty |
| 2 | 489 | 0.63 | 0.76 | 56 | TYR |
| 3 | 188 | 0.47 | 0.75 | 42 | TYR |
| 4 | 95 | 0.47 | 0.81 | 20 | empty |
| 5 | 115 | 0.43 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1568 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6JU7 · Aspergillus oryzae active-tyrosinase copper-depleted 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 6JU7 · PDBe 6JU7 · UniProt A0A1S9DK56
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