Structure of PDB 1dob Chain A

Receptor sequence

>1dobA (length=394) Species: 287 (Pseudomonas aeruginosa)

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQ
GMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVY
GQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRL
DCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYFVQVPLSEKVEDWSDERFWTELKARLPSE
VAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVL
HRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

3D structure

• PDB: 1dob The mobile flavin of 4-OH benzoate hydroxylase.
• Chain: A
• Resolution: 2.0 Å

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 G11 P12 S13 E32 R33 R42 R44 A45 Q102 D159 D286 G298	I8 G11 P12 S13 E32 R33 R42 R44 A45 Q102 D159 D286 G298

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

External links

• PDB: RCSB:1dob, PDBe:1dob, PDBj:1dob
• PDBsum: 1dob
• PubMed: 7939628
• UniProt: P20586|PHHY_PSEAE p-hydroxybenzoate hydroxylase (Gene Name=pobA)