Structure of PDB 1se6 Chain A

Receptor sequence
>1se6A (length=384) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
TISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWLV
TRHDDVRLVTNDPRFGREAVMDRQVTRLAPHFIPARGAVGFLDPPDHTRL
RRSVAAAFTARGVERVRERSRGMLDELVDAMLRAGPPADLTEAVLSPFPI
AVICELMGVPATDRHSMHTWTEMNAYFSDLIGLRSDSAGEDVTSLLGAAV
GRDEITLSEAVGLAVLLQIGGEAVTNNSGQMFHLLLSRPELAERLRSEPE
IRPRAIDELLRWIPHRNAVGLSRIALEDVEIKGVRIRAGDAVYVSYLAAN
RDPEVFPDPDRIDFERSPNPHVSFGFGPHYCPGGMLARLESELLVDAVLD
RVPGLKLAVAPEDVPFKKGALIRGPEALPVTWHH
3D structure
PDB1se6 Binding of Two Flaviolin Substrate Molecules, Oxidative Coupling, and Crystal Structure of Streptomyces coelicolor A3(2) Cytochrome P450 158A2.
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G242 E244 A245 V246 N289 C353 P354 G355 E362 I394
Catalytic site (residue number reindexed from 1) G220 E222 A223 V224 N267 C331 P332 G333 E340 I372
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 A245 H287 R295 Y318 S345 F346 H351 C353 P354 A359 R67 V89 H97 R101 L217 G220 A223 H265 R273 Y296 S323 F324 H329 C331 P332 A337
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1se6, PDBe:1se6, PDBj:1se6
PDBsum1se6
PubMed15659395
UniProtQ9FCA6|C1582_STRCO Biflaviolin synthase CYP158A2 (Gene Name=cyp158a2)

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