Structure of PDB 1iut Chain A Binding Site BS02

Receptor Information
>1iut Chain A (length=394) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQ
GMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVY
GQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRL
DCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSE
VAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVL
HRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
Ligand information
Ligand IDPAB
InChIInChI=1S/C7H7NO2/c8-6-3-1-5(2-4-6)7(9)10/h1-4H,8H2,(H,9,10)
InChIKeyALYNCZNDIQEVRV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ccc(cc1)C(O)=O
ACDLabs 10.04O=C(O)c1ccc(N)cc1
OpenEye OEToolkits 1.5.0c1cc(ccc1C(=O)O)N
FormulaC7 H7 N O2
Name4-AMINOBENZOIC ACID
ChEMBLCHEMBL542
DrugBankDB02362
ZINCZINC000000000920
PDB chain1iut Chain A Residue 396 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1iut pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		L199 Y201 L210 S212 R214 Y222 P293
Binding residue
(residue number reindexed from 1)		L199 Y201 L210 S212 R214 Y222 P293
Annotation score2
Binding affinityMOAD: Kd=24uM
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.
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:1iut, PDBe:1iut, PDBj:1iut
PDBsum1iut
PubMed8555229
UniProtP20586|PHHY_PSEAE p-hydroxybenzoate hydroxylase (Gene Name=pobA)

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