Structure of PDB 1ykj Chain B

Receptor sequence
>1ykjB (length=392) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRGGVLEQ
GMVDLLREAGVDRRMARLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQ
TEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDC
DYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYA
NHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVA
EKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLA
ASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHR
FPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
3D structure
PDB1ykj Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
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:1ykj, PDBe:1ykj, PDBj:1ykj
PDBsum1ykj
PubMed15924424
UniProtP20586|PHHY_PSEAE p-hydroxybenzoate hydroxylase (Gene Name=pobA)

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