Structure of PDB 2whw Chain B

Receptor sequence

>2whwB (length=393) Species: 54571 (Streptomyces venezuelae)

VLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGNEVWLVVGYDRARA
VLADPRFSKDWRNSTTPLTEAEAALNHNMLESDPPRHTRLRKLVAREFTM
RRVELLRPRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGV
PEPDRAAFRVWTDAFVFPDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDL
LSALVRTSDEDGSRLTSEELLGMAHILLVAGHETTVNLIANGMYALLSHP
DQLAALRADMTLLDGAVEEMLRYEGPVESATYRFPVEPVDLDGTVIPAGD
TVLVVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLARLE
ARIAVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWR

3D structure

• PDB: 2whw Selective Oxidation of Carbolide C-H Bonds by an Engineered Macrolide P450 Mono-Oxygenase.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D23 P47 F180 A243 E246 T247 T248 V290 C354 I355 G356 E363 I395
• Catalytic site (residue number reindexed from 1): D10 P34 F167 A230 E233 T234 T235 V277 C341 I342 G343 E350 I382
• Enzyme Commision number: 1.14.15.33: pikromycin 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	M92 L93 H100 R104 A243 T247 T248 T294 R296 A346 F347 G348 H352 C354 I355 G356 A360	M79 L80 H87 R91 A230 T234 T235 T281 R283 A333 F334 G335 H339 C341 I342 G343 A347
BS02	1D4	B	E94 V242 T294	E81 V229 T281	MOAD: Kd=218uM

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
• GO:0033068 macrolide biosynthetic process

External links

• PDB: RCSB:2whw, PDBe:2whw, PDBj:2whw
• PDBsum: 2whw
• PubMed: 19833867
• UniProt: O87605|PIKC_STRVZ Cytochrome P450 monooxygenase PikC (Gene Name=pikC)