Structure of PDB 4z2u Chain A

Receptor sequence
>4z2uA (length=563) Species: 1437882 (Pseudomonas nitroreducens HBP1) [Search protein sequence]
AETDVLIVGAGPAGAMSATLLASLGIRSLMINRWRSTSPGPRSHIINQRT
MEILRDIGLEESAKSLAVPKEYMGEHVYATSLAGEEFGRIPAWASHPQAH
AEHELASPSRYCDLPQLYFEPMVVSEAALRGADVRFLTEYLGHVEDQDGV
TARLLDHVSGAEYEVRAKYIIGADGAHSLVAQNAGLPFEGQMGIGDSGSI
NIEFSADLSSLCEHRKGDMYWMFVAALQMIRPWNKWICVWGYITKEEAKK
IIHEIIGTDEIPVEVGPISTWTINQQYAVRNTSGRVFCMGDAVHRHTPMG
GLGLNTSVQDAYNLAWKLALVLKGTAAPTLLDSYDAERSPVAKQIVERAF
KSLSTFPPVFEALSLPPAPTESEMAEALVRLKDASEEGAKRRAALRKAMD
ATIIGLGGGHGVELNQRYVSRAVFPDGTPDPGFVRDQEFFYQASTRPGAH
LPHVWLTENQRRISTLDLCGKGRFTLLTGLSGAAWKHEAEQVSQSLGIEL
KVCVIGPGQEFVDTYGEYAKISEIGESGALLVRPDMFIAFRAKDASREGL
EQLNVAVKSILGR
3D structure
PDB4z2u A crystal structure of 2-hydroxybiphenyl 3-monooxygenase with bound substrate provides insights into the enzymatic mechanism.
ChainA
Resolution2.5 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 I251 P320
Catalytic site (residue number reindexed from 1) H44 I237 P298
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 FAD A G13 A14 P16 A17 N36 R37 W38 R46 S47 Q120 E143 Y144 A177 D178 W293 G312 D313 G9 A10 P12 A13 N32 R33 W34 R42 S43 Q116 E139 Y140 A173 D174 W271 G290 D291
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:4z2u, PDBe:4z2u, PDBj:4z2u
PDBsum4z2u
PubMed26275805
UniProtO06647

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