Structure of PDB 5foi Chain A

Receptor sequence

>5foiA (length=389) Species: 28040 (Micromonospora griseorubida)

HMVVWPMDRTCAWALPEQYAEFRQRATLVPAKVWDGSPTWLVSRYEHVRA
LLVDPRVTVDPTRQPRLSEADGDGDGFRSMLMLDPPEHTRLRRMFISAFS
VRQVETMRPEIEKIVDGILDRLLALEPPVDILTHLALPMSTQVICHLLGV
PYEDREFFQERSELASRPNDDRSMPALIELVEYLDGLVRTKTAHPDTGLL
GTAVTERLLKGEITHQELVNNAVLLLAAGHETSANQVTLSVLTLLRHPET
AAELREQPELMPNAVDELLRYHSIADGLRRAATADIVLGDHTIRAGDGLI
ILLSSANHDGNTFGAEATFDIHRPARHHVAFGYGPHQCLGQNLARLEMEV
TLGKLFRRVPALRLAQEPDALRVRQGSPIFGIDELLVEW

3D structure

• PDB: 5foi Biochemical and Structural Characterization of Mycci, a Versatile P450 Biocatalyst from the Mycinamicin Biosynthetic Pathway.
• Chain: A
• Resolution: 2.21 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R166 A227 E230 T231 S232 C337 L338 G339 E346 I378
• Catalytic site (residue number reindexed from 1): R167 A228 E231 T232 S233 C338 L339 G340 E347 I379
• Enzyme Commision number: 1.14.-.-

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	M79 L80 H87 R91 L224 A227 G228 T231 L277 R279 A329 F330 H335 C337 L338 G339	M80 L81 H88 R92 L225 A228 G229 T232 L278 R280 A330 F331 H336 C338 L339 G340
BS02	MY8	A	A164 S165 P167 S172 M173 L223	A165 S166 P168 S173 M174 L224	MOAD: Kd=1nM

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

External links

• PDB: RCSB:5foi, PDBe:5foi, PDBj:5foi
• PDBsum: 5foi
• PubMed: 27420774
• UniProt: Q83WF5|MYCCI_MICGR Mycinamicin VIII C21 methyl hydroxylase (Gene Name=mycCI)