Structure of PDB 2bvj Chain B

Receptor sequence
>2bvjB (length=391) Species: 54571 (Streptomyces venezuelae) [Search protein sequence]
SPPVLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGDEVWLVVGYDR
ARAVLADPRFSKDWRNSTTPLLNHNMLESDPPRHTRLRKLVAREFTMRRV
ELLRPRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGVPEP
DRAAFRVWTDAFVFPDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDLLSA
LVRTSDEDGSRLTSEELLGMAHILLVAGHETTVNLIANGMYALLSHPDQL
AALRADMTLLDGAVEEMLRYEGPVESATYRFPVEPVDLDGTVIPAGDTVL
VVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLARLEARI
AVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWRR
3D structure
PDB2bvj The Structural Basis for Substrate Anchoring, Active Site Selectivity, and Product Formation by P450 Pikc from Streptomyces Venezuelae.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) D13 P37 F164 A227 E230 T231 T232 V274 C338 I339 G340 E347 I379
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 F111 A243 G244 T247 T248 L251 T294 R296 A346 F347 G348 H352 C354 I355 G356 A360 M76 L77 H84 R88 F95 A227 G228 T231 T232 L235 T278 R280 A330 F331 G332 H336 C338 I339 G340 A344
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

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Molecular Function

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Biological Process
External links
PDB RCSB:2bvj, PDBe:2bvj, PDBj:2bvj
PDBsum2bvj
PubMed16825192
UniProtO87605|PIKC_STRVZ Cytochrome P450 monooxygenase PikC (Gene Name=pikC)

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