Structure of PDB 1foh Chain D

Receptor sequence

>1fohD (length=654) Species: 5554 (Cutaneotrichosporon cutaneum) [Search protein sequence]

TKYSESYCDVLIVGAGPAGLMAARVLSEYVRQKPDLKVRIIDKRSTKVYN
GQADGLQCRTLESLKNLGLADKILSEANDMSTIALYNPDENGHIRRTDRI
PDTLPGISRYHQVVLHQGRIERHILDSIAEISDTRIKVERPLIPEKMEID
SSKAEDPEAYPVTMTLRYMSDHESTPLQFGHKTENSLFHSNLQTQEEEDA
NYRLPEGKEAGEIETVHCKYVIGCDGGHSWVRRTLGFEMIGEQTDYIWGV
LDAVPASNFPDIRSRCAIHSAESGSIMIIPRENNLVRFYVQLQVDRTKFT
PEVVIANAKKIFHPYTFDVQQLDWFTAYHIGQRVTEKFSKDERVFIAGDA
CHTHSPKAGQGMNTSMMDTYNLGWKLGLVLTGRAKRDILKTYEEERHAFA
QALIDFDHQFSRLFSGRPAKDVADEMGVSMDVFKEAFVKGNEFASGTAIN
YDENLVTDKKSSKQELAKNCVVGTRFKSQPVVRHSEGLWMHFGDRLVTDG
RFRIIVFAGKATDATQMSRIKKFSAYLDSENSVISLYTPKVSDRNSRIDV
ITIHSCHRDDIEMHDFPAPALHPKWQYDFIYADCDSWHHPHPKSYQAWGV
DETKGAVVVVRPDGYTSLVTDLEGTAEIDRYFSGILVEPKEKSGAQTEAD
WTKS

3D structure

PDB

1foh The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis.

Chain

Resolution

2.4 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 P356
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	D	G16 P17 A18 D42 K43 R44 N50 Q52 A53 D54 G55 N191 C224 D225 G226 Y289 G356 D357 P364 G367 G369 M370 N371 S373	G16 P17 A18 D42 K43 R44 N50 Q52 A53 D54 G55 N191 C224 D225 G226 Y289 G348 D349 P356 G359 G361 M362 N363 S365
BS02	IPH	D	D54 G55 Q112 V114 I279 Y289 G367	D54 G55 Q112 V114 I279 Y289 G359

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:1foh, PDBe:1foh, PDBj:1foh
PDBsum	1foh
PubMed	9634698
UniProt	P15245\|PHHY_CUTCT Phenol hydroxylase

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