Research workbench
Crystal structure of the copper-free streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein in the monoclinic crystal
Analyse Crystal structure of the copper-free streptomyces castaneoglobisporus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WX5
- Type
- protein
- Length
- 694 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosinase; Melc
- EC
- 1.14.18.1
- UniProt
- Q83WS2, Q83WS1
- Ligands
- NA, CL
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase (EC 1.14.18.1) | protein | 275 | 38% helix, 4% strand | Q83WS2 |
| B | Melc | protein | 71 | 17% helix, 45% strand | Q83WS1 |
| C | Tyrosinase (EC 1.14.18.1) | protein | 273 | 41% helix, 5% strand | Q83WS2 |
| D | Melc | protein | 75 | 16% helix, 43% strand | Q83WS1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 528 | 0.72 | 0.81 | 44 | empty |
| 2 | 148 | 0.50 | 0.79 | 31 | empty |
| 3 | 117 | 0.43 | 0.77 | 24 | empty |
| 4 | 76 | 0.37 | 0.77 | 18 | empty |
| 5 | 62 | 0.32 | 0.75 | 14 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1013 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 989 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 614 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1WX5 · Crystal Structure of the copper-free Streptomyces castaneoglobisporus tyrosinase… · 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 1WX5 · PDBe 1WX5 · UniProt Q83WS2 · UniProt Q83WS1
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