Structure of PDB 1ykj Chain B Binding Site BS03

Receptor Information
>1ykj Chain B (length=392) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRGGVLEQ
GMVDLLREAGVDRRMARLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQ
TEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDC
DYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYA
NHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVA
EKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLA
ASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHR
FPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
Ligand information
Ligand IDPSL
InChIInChI=1S/H2O7S2/c1-8(2,3)7-9(4,5)6/h(H,1,2,3)(H,4,5,6)/p-2
InChIKeyVFNGKCDDZUSWLR-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)OS(=O)(=O)[O-]
CACTVS 3.341[O-][S](=O)(=O)O[S]([O-])(=O)=O
ACDLabs 10.04[O-]S(=O)(=O)OS([O-])(=O)=O
FormulaO7 S2
NamePYROSULFATE
ChEMBL
DrugBank
ZINC
PDB chain1ykj Chain B Residue 715 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ykj Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		R2033 A2125 E2126 R2128
Binding residue
(residue number reindexed from 1)		R33 A123 E124 R126
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H2072 Y2201 P2293 K2297 Y2385
Catalytic site (residue number reindexed from 1) H70 Y199 P291 K295 Y383
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ykj, PDBe:1ykj, PDBj:1ykj
PDBsum1ykj
PubMed15924424
UniProtP20586|PHHY_PSEAE p-hydroxybenzoate hydroxylase (Gene Name=pobA)

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