Research workbench
Phenol hydroxylase from trichosporon cutaneum
Analyse Phenol hydroxylase from trichosporon cutaneum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FOH
- Type
- protein
- Length
- 2,610 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenol hydroxylase
- EC
- 1.14.13.7
- UniProt
- P15245
- Ligands
- FAD, IPH
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenol hydroxylase (EC 1.14.13.7) | protein | 649 | 29% helix, 27% strand | P15245 |
| B | Phenol hydroxylase (EC 1.14.13.7) | protein | 651 | 30% helix, 26% strand | P15245 |
| C | Phenol hydroxylase (EC 1.14.13.7) | protein | 656 | 28% helix, 25% strand | P15245 |
| D | Phenol hydroxylase (EC 1.14.13.7) | protein | 654 | 28% helix, 26% strand | P15245 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- IPH · Phenol · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 564 | 0.84 | 0.90 | 75 | FAD |
| 2 | 705 | 0.83 | 0.87 | 102 | FAD, IPH |
| 3 | 642 | 0.74 | 0.81 | 79 | empty |
| 4 | 1194 | 0.74 | 0.77 | 121 | empty |
| 5 | 673 | 0.73 | 0.80 | 62 | FAD |
Interfaces
4 interfaces between chains.
- B–D · 2006 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 1996 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 402 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 107 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 P15245
- Elsewhere: RCSB PDB 1FOH · PDBe 1FOH · UniProt P15245
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