Structure of PDB 1pbb Chain A Binding Site BS02

Receptor Information
>1pbb Chain A (length=391) Species: 294 (Pseudomonas fluorescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQ
GMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVY
GQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRL
DCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAE
VAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVL
HRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYE
Ligand information
Ligand IDDOB
InChIInChI=1S/C7H6O4/c8-4-1-2-5(7(10)11)6(9)3-4/h1-3,8-9H,(H,10,11)
InChIKeyUIAFKZKHHVMJGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)c1ccc(O)cc1O
CACTVS 3.341OC(=O)c1ccc(O)cc1O
OpenEye OEToolkits 1.5.0c1cc(c(cc1O)O)C(=O)O
FormulaC7 H6 O4
Name2,4-DIHYDROXYBENZOIC ACID
ChEMBLCHEMBL328910
DrugBankDB02839
ZINCZINC000000388544
PDB chain1pbb 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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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
Resolution2.5 Å
Binding residue
(original residue number in PDB)		V47 Y201 L210 S212 R214 Y222 P293 T294
Binding residue
(residue number reindexed from 1)		V47 Y201 L210 S212 R214 Y222 P293 T294
Annotation score2
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:1pbb, PDBe:1pbb, PDBj:1pbb
PDBsum1pbb
PubMed7520279
UniProtP00438|PHHY_PSEFL p-hydroxybenzoate hydroxylase (Gene Name=pobA)

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