Research workbench
Crystal structure of the MET2-form of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking in cupric sulfate solution for 80 hours
Analyse Crystal structure of the MET2-form of the copper-bound tyrosinase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZMY
- Type
- protein
- Length
- 355 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosinase; Caddie
- EC
- 1.14.18.1
- UniProt
- Q83WS2
- Ligands
- CU, NO3
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase (EC 1.14.18.1) | protein | 277 | 41% helix, 5% strand | Q83WS2 |
| B | Caddie | protein | 78 | 15% helix, 42% strand | — |
Ligands and binding sites
- CU · Copper (II) ion · metal · 5 copies · chains A, B
- NO3 · Nitrate ion · ion · 6 copies · chains A, B
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 | 135 | 0.49 | 0.79 | 28 | empty |
| 2 | 59 | 0.31 | 0.75 | 14 | empty |
| 3 | 54 | 0.28 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1173 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2ZMY · Crystal structure of the met2-form of the copper-bound tyrosinase in complex with a… · 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
- Elsewhere: RCSB PDB 2ZMY · PDBe 2ZMY · UniProt Q83WS2
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