Structure of PDB 2nz5 Chain B

Receptor sequence

>2nz5B (length=399) Species: 100226 (Streptomyces coelicolor A3(2))

PPPVRDWPALDLDGPEFDPVLAELMREGPLTRVRLPHGEGWAWLATRYDD
VKAITNDPRFGRAEVTQRQITRLAPHFKPRPGSLAFADQPDHNRLRRAVA
GAFTVGATKRLRPRAQEILDGLVDGILAEGPPADLVERVLEPFPIAVVSE
VMGVPAADRERVHSWTRQIISTSGGAEAAERAKRGLYGWITETVRARAGS
EGGDVYSMLGAAVGRGEVGETEAVGLAGPLQIGGEAVTHNVGQMLYLLLT
RRELMARMRERPGARGTALDELLRWISHRTSVGLARIALEDVEVHGTRIA
AGEPVYVSYLAANRDPDVFPDPDRIDLDRDPNPHLAYGNGHHFCTGAVLA
RMQTELLVDTLLERLPGLRLAVPAEQVAWRRKTMIRGPRTLPCTWHHHH

3D structure

• PDB: 2nz5 Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2.
• Chain: B
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S183 G245 E247 A248 V249 T292 C356 T357 G358 Q365 I397
• Catalytic site (residue number reindexed from 1): S171 G233 E235 A236 V237 T280 C344 T345 G346 Q353 I385
• 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	R74 L96 H104 G245 A248 L296 A348 Y349 H354 C356 T357	R62 L84 H92 G233 A236 L284 A336 Y337 H342 C344 T345
BS02	226	B	R291 L296 M396	R279 L284 M384	MOAD: Kd=10.5uM
BS03	226	B	R92 K195 Y199	R80 K183 Y187	MOAD: Kd=10.5uM

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:2nz5, PDBe:2nz5, PDBj:2nz5
• PDBsum: 2nz5
• PubMed: 17614370
• UniProt: Q9KZF5|C1581_STRCO Biflaviolin synthase CYP158A1 (Gene Name=cyp158a1)