Structure of PDB 2d09 Chain A

Receptor sequence

>2d09A (length=404) Species: 100226 (Streptomyces coelicolor A3(2))

ETISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWL
VTRHDDVRLVTNDPRFGREAVMDRQVTRLAPHFIPARGAVGFLDPPDHTR
LRRSVAAAFTARGVERVRERSRGMLDELVDAMLRAGPPADLTEAVLSPFP
IAVICELMGVPATDRHSMHTWTQLILSSSHGAEVSERAKNEMNAYFSDLI
GLRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQIGGEAVTNNSGQM
FHLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALEDVEI
KGVRIRAGDAVYVSYLAANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYC
PGGMLARLESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEALPVT
WAAA

3D structure

• PDB: 2d09 Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S180 G242 E244 A245 V246 N289 C353 P354 G355 E362 I394
• Catalytic site (residue number reindexed from 1): S177 G239 E241 A242 V243 N286 C350 P351 G352 E359 I391
• Enzyme Commision number: 1.14.19.69: biflaviolin synthase.

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	R71 V93 H101 R105 L239 G242 G243 H287 R295 Y318 S345 F346 H351 C353 P354 G355 A359	R68 V90 H98 R102 L236 G239 G240 H284 R292 Y315 S342 F343 H348 C350 P351 G352 A356
BS02	FLV	A	R288 G292 L293	R285 G289 L290	MOAD: Kd=7.3uM
BS03	FLV	A	I87 P88 R288 G292 L393	I84 P85 R285 G289 L390	MOAD: Kd=7.3uM

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:0042440 pigment metabolic process

External links

• PDB: RCSB:2d09, PDBe:2d09, PDBj:2d09
• PDBsum: 2d09
• PubMed: 16239228
• UniProt: Q9FCA6|C1582_STRCO Biflaviolin synthase CYP158A2 (Gene Name=cyp158a2)