Structure of PDB 1pn0 Chain C

Receptor sequence

>1pn0C (length=656) Species: 5554 (Cutaneotrichosporon cutaneum) [Search protein sequence]

TKYSESYCDVLIVGAGPAGLMAARVLSEYVRQKPDLKVRIIDKRSTKVYN
GQADGLQCRTLESLKNLGLADKILSEANDMSTIALYNPDENGHIRRTDRI
PDTLPGISRYHQVVLHQGRIERRILDSIAEISDTRIKVERPLIPEKMEID
SSKAEDPEAYPVTMTLRYMSEDESTPLQFGHKTENGLFRSNLQTQEEEDA
NYRLPEGKEAGEIETVHCKYVIGCDGGHSWVRRTLGFEMIGEQTDYIWGV
LDAVPASNFPDIRSRCAIHSAESGSIMIIPRENNLVRFYVQLQARVDRTK
FTPEVVIANAKKIFHPYTFDVQQLDWFTAYHIGQRVTEKFSKDERVFIAG
DACHTHSPKAGQGMNTSMMDTYNLGWKLGLVLTGRAKRDILKTYEEERQP
FAQALIDFDHQFSRLFSGRPAKDVADEMGVSMDVFKEAFVKGNEFASGTA
INYDENLVTDKKSSKQELAKNCVVGTRFKSQPVVRHSEGLWMHFGDRLVT
DGRFRIIVFAGKATDATQMSRIKKFAAYLDSENSVISRYTPKGADRNSRI
DVITIHSCHRDDIEMHDFPAPALHPKWQYDFIYADCDSWHHPHPKSYQAW
GVDETKGAVVVVRPDGYTSLVTDLEGTAEIDRYFSGILVEPKEKSGAQTE
ADWTKS

3D structure

PDB

1pn0 High-resolution structure of phenol hydroxylase and correction of sequence errors.

Chain

Resolution

1.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D54 R281 Y289 P364
Catalytic site (residue number reindexed from 1)	D54 R281 Y289 P358
Enzyme Commision number	1.14.13.7: phenol 2-monooxygenase (NADPH).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	C	V13 G14 P17 A18 D42 K43 R44 N50 Q52 A53 D54 G55 R189 D225 G226 Y289 G356 D357 P364 G367 Q368 G369 M370 N371 S373	V13 G14 P17 A18 D42 K43 R44 N50 Q52 A53 D54 G55 R189 D225 G226 Y289 G350 D351 P358 G361 Q362 G363 M364 N365 S367
BS02	IPH	C	D54 Q112 M277 I279 Y289 P364 A366 G367	D54 Q112 M277 I279 Y289 P358 A360 G361

Gene Ontology

	Molecular Function
GO:0004497	monooxygenase activity
GO:0016491	oxidoreductase activity
GO:0016709	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0018662	phenol 2-monooxygenase activity
GO:0071949	FAD binding

	Biological Process
GO:0009056	catabolic process
GO:0019336	phenol-containing compound catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:1pn0, PDBe:1pn0, PDBj:1pn0
PDBsum	1pn0
PubMed	12925790
UniProt	P15245\|PHHY_CUTCT Phenol hydroxylase

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