Structure of PDB 1jio Chain A

Receptor sequence
>1jioA (length=403) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence]
TTVPDLESDSFHVDWYRTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAA
LSDLRLSSDPKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRL
RKLVSQEFTVRRVEAMRPRVEQITAELLDEVGDSGVVDIVDRFAHPLPIK
VICELLGVDEKYRGEFGRWSSEILVMDPERAEQRGQAAREVVNFILDLVE
RRRTEPGDDLLSALIRVQDDDDGRLSADELTSIALVLLLAGFEASVSLIG
IGTYLLLTHPDQLALVRRDPSALPNAVEEILRYIAPPETTTRFAAEEVEI
GGVAIPQYSTVLVANGAANRDPKQFPDPHRFDVTRDTRGHLSFGQGIHFC
MGRPLAKLEGEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVR
LDG
3D structure
PDB1jio Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V176 A241 E244 A245 S246 C351 M352 G353 E360 L392
Catalytic site (residue number reindexed from 1) V175 A240 E243 A244 S245 C350 M351 G352 E359 L391
Enzyme Commision number 1.14.15.35: 6-deoxyerythronolide B hydroxylase.
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 HEM A M90 G91 H98 R102 F109 A241 G242 A245 P288 R293 S343 F344 H349 C351 G353 M89 G90 H97 R101 F108 A240 G241 A244 P287 R292 S342 F343 H348 C350 G352
BS02 DEB A A74 A241 A73 A240
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:1901115 erythromycin biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1jio, PDBe:1jio, PDBj:1jio
PDBsum1jio
PubMed11469860
UniProtQ00441|CPXJ_SACEN 6-deoxyerythronolide B hydroxylase (Gene Name=eryF)

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