Structure of PDB 1iut Chain A

Receptor sequence
>1iutA (length=394) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQ
GMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVY
GQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRL
DCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSE
VAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVL
HRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
3D structure
PDB1iut pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 V47 Q102 D159 D286 A296 G298 L299 N300 I8 G11 P12 S13 E32 R33 R42 R44 A45 V47 Q102 D159 D286 A296 G298 L299 N300
BS02 PAB A L199 Y201 L210 S212 R214 Y222 P293 L199 Y201 L210 S212 R214 Y222 P293 MOAD: Kd=24uM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1iut, PDBe:1iut, PDBj:1iut
PDBsum1iut
PubMed8555229
UniProtP20586|PHHY_PSEAE p-hydroxybenzoate hydroxylase (Gene Name=pobA)

[Back to BioLiP]