Structure of PDB 1pbb Chain A

Receptor sequence
>1pbbA (length=391) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQ
GMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVY
GQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRL
DCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAE
VAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVL
HRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
3D structure
PDB1pbb Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring
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) 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 I8 P12 S13 E32 R33 R42 R44 A45 Q102 D159 I164 G285 D286 G298 I8 P12 S13 E32 R33 R42 R44 A45 Q102 D159 I164 G285 D286 G298
BS02 DOB A V47 Y201 L210 S212 R214 Y222 P293 T294 V47 Y201 L210 S212 R214 Y222 P293 T294
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:1pbb, PDBe:1pbb, PDBj:1pbb
PDBsum1pbb
PubMed7520279
UniProtP00438|PHHY_PSEFL p-hydroxybenzoate hydroxylase (Gene Name=pobA)

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