Structure of PDB 1se6 Chain B

Receptor sequence

>1se6B (length=402) Species: 100226 (Streptomyces coelicolor A3(2))

TISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWLV
TRHDDVRLVTNDPRFGREAVMDRQVTRLAPHFIPARGAVGFLDPPDHTRL
RRSVAAAFTARGVERVRERSRGMLDELVDAMLRAGPPADLTEAVLSPFPI
AVICELMGVPATDRHSMHTWTQLILSSSHGAEVSERAKNEMNAYFSDLIG
LRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQIGGEAVTNNSGQMF
HLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALEDVEIK
GVRIRAGDAVYVSYLAANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYCP
GGMLARLESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEALPVTW
HH

3D structure

• PDB: 1se6 Binding of Two Flaviolin Substrate Molecules, Oxidative Coupling, and Crystal Structure of Streptomyces coelicolor A3(2) Cytochrome P450 158A2.
• Chain: B
• Resolution: 1.75 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): S176 G238 E240 A241 V242 N285 C349 P350 G351 E358 I390
• 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	B	R71 V93 H101 R105 L239 G242 A245 V246 N249 H287 R295 Y318 S345 F346 H351 C353 P354	R67 V89 H97 R101 L235 G238 A241 V242 N245 H283 R291 Y314 S341 F342 H347 C349 P350

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:1se6, PDBe:1se6, PDBj:1se6
• PDBsum: 1se6
• PubMed: 15659395
• UniProt: Q9FCA6|C1582_STRCO Biflaviolin synthase CYP158A2 (Gene Name=cyp158a2)