Structure of PDB 1foh Chain C

Receptor sequence
>1fohC (length=656) Species: 5554 (Cutaneotrichosporon cutaneum) [Search protein sequence]
TKYSESYCDVLIVGAGPAGLMAARVLSEYVRQKPDLKVRIIDKRSTKVYN
GQADGLQCRTLESLKNLGLADKILSEANDMSTIALYNPDENGHIRRTDRI
PDTLPGISRYHQVVLHQGRIERHILDSIAEISDTRIKVERPLIPEKMEID
SSKAEDPEAYPVTMTLRYMSDHESTPLQFGHKTENSLFHSNLQTQEEEDA
NYRLPEGKEAGEIETVHCKYVIGCDGGHSWVRRTLGFEMIGEQTDYIWGV
LDAVPASNFPDIRSRCAIHSAESGSIMIIPRENNLVRFYVQLRVDRTKFT
PEVVIANAKKIFHPYTFDVQQLDWFTAYHIGQRVTEKFSKDERVFIAGDA
CHTHSPKAGQGMNTSMMDTYNLGWKLGLVLTGRAKRDILKTYEEERHAFA
QALIDFDHQFSRLFSGRPAKDVADEMGVSMDVFKEAFVKGNEFASGTAIN
YDENLVTDKKSSKQELAKNCVVGTRFKSQPVVRHSEGLWMHFGDRLVTDG
RFRIIVFAGKATDATQMSRIKKFSAYLDSENSVISLYTPKVSDRNSRIDV
ITIHSCHRDDIEMHDFPAPALHPKWQYDFIYADCDSWHHPHPKSYQAWGV
DETKGAVVVVRPDGYTSLVTDLEGTAEIDRYFSGILVEPKEKSGAQTEAD
WTKSTA
3D structure
PDB1foh 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.
ChainC
Resolution2.4 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
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1foh, PDBe:1foh, PDBj:1foh
PDBsum1foh
PubMed9634698
UniProtP15245|PHHY_CUTCT Phenol hydroxylase

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