Structure of PDB 2y98 Chain A

Receptor sequence

>2y98A (length=393) Species: 28040 (Micromonospora griseorubida)

EPRAYPFNDVHGLTLAGRYGELQETEPVSRVRPPYGEEAWLVTRYEDVRA
VLGDGRFVRGPSMTRDEPRTRPEMVKGGLLSMDPPEHSRLRRLVVKAFTA
RRAESLRPRAREIAHELVDQMAATGQPADLVAMFARQLPVRVICELLGVP
SADHDRFTRWSGAFLSTAEVTAEEMQEAAEQAYAYMGDLIDRRRKEPTDD
LVSALVQARDQQDSLSEQELLDLAIGLLVAGYESTTTQIADFVYLLMTRP
ELRRQLLDRPELIPSAVEELTRWVPLGVGTAFPRYAVEDVTLRGVTIRAG
EPVLASTGAANRDQAQFPDADRIDVDRTPNQHLGFGHGVHHCLGAPLARV
ELQVALEVLLQRLPGIRLGIPETQLRWSEGMLLRGPLELPVVW

3D structure

• PDB: 2y98 Substrate Recognition by the Multifunctional Cytochrome P450 Mycg in Mycinamicin Hydroxylation and Epoxidation Reactions.
• Chain: A
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S170 A234 E237 S238 T239 V282 C346 L347 G348 E355 L387
• Catalytic site (residue number reindexed from 1): S166 A230 E233 S234 T235 V278 C342 L343 G344 E351 L383
• 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	L83 L84 H91 R95 F102 A234 G235 S238 T239 Q242 F286 R288 F339 H344 C346 L347 G348 A352	L79 L80 H87 R91 F98 A230 G231 S234 T235 Q238 F282 R284 F335 H340 C342 L343 G344 A348
BS02	MIV	A	R75 V79 G81 L84 F168 S170 V174 M179 V233 A234 L386	R71 V75 G77 L80 F164 S166 V170 M175 V229 A230 L382

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:2y98, PDBe:2y98, PDBj:2y98
• PDBsum: 2y98
• PubMed: 22952225
• UniProt: Q59523|MYCG_MICGR Mycinamicin IV hydroxylase/epoxidase (Gene Name=mycG)