Research workbench
F194Y mutant of the dye-decolorizing peroxidase (dyp) from pleurotus ostreatus
Analyse F194Y mutant of the dye-decolorizing peroxidase (dyp) from pleurotus ostreatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FSK
- Type
- protein
- Length
- 968 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dyp-type peroxidase
- UniProt
- A0A067N4E7
- Ligands
- HEM
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dyp-type peroxidase | protein | 484 | 32% helix, 19% strand | A0A067N4E7 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.84 | 0.94 | 37 | HEM |
| 2 | 750 | 0.80 | 0.84 | 86 | HEM |
| 3 | 1062 | 0.72 | 0.76 | 84 | empty |
| 4 | 295 | 0.57 | 0.77 | 45 | empty |
| 5 | 82 | 0.36 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 466 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
- 6FSK · F194Y mutant of the Dye-decolorizing peroxidase (DYP) from Pleurotus ostreatus · 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 A0A067N4E7
- Elsewhere: RCSB PDB 6FSK · PDBe 6FSK · UniProt A0A067N4E7
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