Structure of PDB 2yca Chain A

Receptor sequence

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

EPRAYPFNDVHGLTLAGRYGELQETEPVSRVRPPYGEEAWLVTRYEDVRA
VLGDGRFVRGPSMTRDEPRTRPEMVKGGLLSMDPPEHSRLRRLVVKAFTA
RRAESLRPRAREIAHELVDQMAATGQPADLVAMFARQLPVRVICELLGVP
SADHDRFTRWSGAFLSTAEVTAEEMQEAAEQAYAYMGDLIDRRRKEPTDD
LVSALVQARDQQDSLSEQELLDLAIGLLVAGYESTTTQIADFVYLLMTRP
ELRRQLLDRPELIPSAVEELTRWVPLGVGTAFPRYAVEDVTLRGVTIRAG
EPVLASTGAANRDQAQFPDADRIDVDRTPNQHLGFGHGVHHCLGAPLARV
ELQVALEVLLQRLPGIRLGIPETQLRWSEGMLLRGPLELPVVW

3D structure

• PDB: 2yca Substrate Recognition by the Multifunctional Cytochrome P450 Mycg in Mycinamicin Hydroxylation and Epoxidation Reactions.
• Chain: A
• Resolution: 1.8 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	L84 H91 R95 F102 A234 G235 S238 T239 Q242 R288 F339 G340 H344 C346 L347 G348 A352	L80 H87 R91 F98 A230 G231 S234 T235 Q238 R284 F335 G336 H340 C342 L343 G344 A348
BS02	ZM3	A	L84 Y187 V233 G281 T284	L80 Y183 V229 G277 T280

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