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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: 1PN0
Type: protein
Length: 2,616 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenol 2-monooxygenase
EC: 1.14.13.7
UniProt: P15245
Ligands: FAD, IPH, CL
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phenol 2-monooxygenase (EC 1.14.13.7)	protein	652	29% helix, 26% strand	P15245
C, D	Phenol 2-monooxygenase (EC 1.14.13.7)	protein	656	30% 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
CL · Chloride ion · ion · 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, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	600	0.85	0.91	80	FAD, IPH
2	734	0.84	0.88	98	FAD, IPH
3	848	0.77	0.81	99	empty
4	1111	0.74	0.77	107	CL
5	989	0.74	0.77	93	CL

Interfaces

4 interfaces between chains.

B–D · 1996 Å² buried · 25 hydrogen bonds · protein-protein
A–C · 1991 Å² buried · 26 hydrogen bonds · protein-protein
C–D · 437 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 99 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1PN0 · Phenol hydroxylase from Trichosporon cutaneum · the same entry in another collection · chain A against A, TM-score 1.00
P15245 · AlphaFold monomer V2.0 prediction for phenol hydroxylase (P15245) · a predicted model of the same protein · chain C 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 P15245
Elsewhere: RCSB PDB 1PN0 · PDBe 1PN0 · UniProt P15245

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