Structure of PDB 4cy8 Chain B

Receptor sequence
>4cy8B (length=535) Species: 1437882 (Pseudomonas nitroreducens HBP1) [Search protein sequence]
SAETDVLIVGAGPAGAMSATLLASLGIRSLMINRWRSTSPGPRSHIINQR
TMEILRDIGLEESAKSLAVPKEYMGEHVYATSLAGEEFGRIPAWASHPQA
HAEHELASPSRYCDLPQLYFEPMVVSEAALRGADVRFLTEYLGHVEDQDG
VTARLLDHVSGAEYEVRAKYIIGADGAHSLVAQNAGLPFEGSINIEFSAD
DMYWMFRGVAALRMKWICVEEAKKIIHEIIGTDEIPEVGPISTWTINQQY
AVRNTSGRVFCMGDAVHRHTPMGGLGLNTSVQDAYNLAWKLALVLKGQAA
PTLLDSYDAERSPVAKQIVERAFKSLSTFPPVFEALSLPPATESEMAEAL
VRLKDASEEGAKRRAALRKAMDATIIGLGGGHGVELNQRYVSRAVFPDGT
PDPGFVRDQEFFYQASTRPGAHLPHVWLTENQRRISTLDLCGKGRFTLLT
GLSGAAWKHEAEQVSQSLGIELKVCVIGPGQEFVDTYGEYAKISEIGESG
ALLVRPDMFIAFRAKDASREGLEQLNVAVKSILGR
3D structure
PDB4cy8 Structures of the Apo and Fad-Bound Forms of 2-Hydroxybiphenyl 3-Monooxygenase (Hbpa) Locate Activity Hotspots Identified by Using Directed Evolution.
ChainB
Resolution2.03 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H48 G237 I251 P320
Catalytic site (residue number reindexed from 1) H45 G208 I217 P271
Enzyme Commision number 1.14.13.44: 2-hydroxybiphenyl 3-monooxygenase.
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 FDA B G13 G15 P16 A17 N36 R37 W38 R46 S47 H48 I49 Q120 Y144 A177 D178 G312 D313 P320 G323 G325 L326 N327 G10 G12 P13 A14 N33 R34 W35 R43 S44 H45 I46 Q117 Y141 A174 D175 G263 D264 P271 G274 G276 L277 N278
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0071949 FAD binding

View graph for
Molecular Function
External links
PDB RCSB:4cy8, PDBe:4cy8, PDBj:4cy8
PDBsum4cy8
PubMed25737306
UniProtO06647

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