Research workbench
Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes
Analyse Crystal structure of the copper-bound tyrosinase in complex with a caddie… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZWF
- Type
- protein
- Length
- 348 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosinase; Melc
- EC
- 1.14.18.1
- UniProt
- Q83WS2, Q83WS1
- Ligands
- CU, NO3
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase (EC 1.14.18.1) | protein | 276 | 41% helix, 4% strand | Q83WS2 |
| B | Melc | protein | 72 | 17% helix, 39% strand | Q83WS1 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 4 copies · chains A, B
- NO3 · Nitrate ion · ion · 5 copies · chains A, B
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 | 144 | 0.50 | 0.79 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1026 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 2ZWF · Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from… · 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 Q83WS2
- Every structure of UniProt Q83WS1
- Elsewhere: RCSB PDB 2ZWF · PDBe 2ZWF · UniProt Q83WS2 · UniProt Q83WS1
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