Research workbench
Tyrosinase from burkholderia thailandensis (bttyr) at high pH condition
Analyse Tyrosinase from burkholderia thailandensis (bttyr) at high pH condition in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZRE
- Type
- protein
- Length
- 1,415 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosinase
- EC
- 1.14.18.1
- UniProt
- Q2T7K1
- Ligands
- CU, O
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosinase (EC 1.14.18.1) | protein | 469 | 37% helix, 18% strand | Q2T7K1 |
| B | Tyrosinase (EC 1.14.18.1) | protein | 474 | 38% helix, 18% strand | Q2T7K1 |
| C | Tyrosinase (EC 1.14.18.1) | protein | 472 | 37% helix, 16% strand | Q2T7K1 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 6 copies · chains A, B, C
- O · Oxygen atom · ion · 3 copies · chains A, B, C
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.77 | 0.95 | 26 | empty |
| 2 | 126 | 0.77 | 0.95 | 27 | empty |
| 3 | 110 | 0.76 | 0.96 | 22 | empty |
| 4 | 915 | 0.71 | 0.76 | 77 | empty |
| 5 | 634 | 0.66 | 0.75 | 71 | empty |
Interfaces
2 interfaces between chains.
- A–B · 265 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 245 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5ZRE · Tyrosinase from Burkholderia thailandensis (BtTYR) at high pH condition · 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 Q2T7K1
- Elsewhere: RCSB PDB 5ZRE · PDBe 5ZRE · UniProt Q2T7K1
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