Structure of PDB 1oxa Chain A

Receptor sequence

>1oxaA (length=403) Species: 1836 (Saccharopolyspora erythraea)

ATVPDLESDSFHVDWYSTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAA
LSDLRLSSDPKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRL
RKLVSQEFTVRRVEAMRPRVEQITAELLDEVGDSGVVDIVDRFAHPLPIK
VICELLGVDEAARGAFGRWSSEILVMDPERAEQRGQAAREVVNFILDLVE
RRRTEPGDDLLSALISVQDDDDGRLSADELTSIALVLLLAGFEASVSLIG
IGTYLLLTHPDQLALVRADPSALPNAVEEILRYIAPPETTTRFAAEEVEI
GGVAIPQYSTVLVANGAANRDPSQFPDPHRFDVTRDTRGHLSFGQGIHFC
MGRPLAKLEGEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVR
LDG

3D structure

• PDB: 1oxa Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
• Chain: A
• Resolution: 2.1 Å

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 A245 P288 R293 S343 F344 H349 C351 G353	M89 G90 H97 R101 F108 A244 P287 R292 S342 F343 H348 C350 G352
BS02	DEB	A	G91 P288	G90 P287

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

External links

• PDB: RCSB:1oxa, PDBe:1oxa, PDBj:1oxa
• PDBsum: 1oxa
• PubMed: 7749919
• UniProt: Q00441|CPXJ_SACEN 6-deoxyerythronolide B hydroxylase (Gene Name=eryF)