Structure of PDB 1bgn Chain A

Receptor sequence
>1bgnA (length=391) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQ
GMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVY
GQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRL
DCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAE
VAEKLVTGPSLEKSIAPLTSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVL
HRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
3D structure
PDB1bgn Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H72 Y201 P293 K297 Y385
Catalytic site (residue number reindexed from 1) H72 Y201 P293 K297 Y385
Enzyme Commision number 1.14.13.2: 4-hydroxybenzoate 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 G11 P12 S13 E32 R33 R42 R44 A45 G46 V47 Q102 D159 D286 P293 A296 G298 L299 N300 G11 P12 S13 E32 R33 R42 R44 A45 G46 V47 Q102 D159 D286 P293 A296 G298 L299 N300
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:0018659 4-hydroxybenzoate 3-monooxygenase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
GO:0106356 4-hydroxybenzoate 3-monooxygenase (NADPH) activity
Biological Process
GO:0009056 catabolic process
GO:0043639 benzoate catabolic process
GO:0043640 benzoate catabolic process via hydroxylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1bgn, PDBe:1bgn, PDBj:1bgn
PDBsum1bgn
PubMed9694855
UniProtP00438|PHHY_PSEFL p-hydroxybenzoate hydroxylase (Gene Name=pobA)

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