Structure of PDB 3ejd Chain B

Receptor sequence
>3ejdB (length=382) Species: 1423 (Bacillus subtilis) [Search protein sequence]
SEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDARFKV
RTPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTESYQ
PYIIETVHHLLDQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDREQLK
EWAASLIQTIDFTRSRKALTEGNIMAVQAMAYFKELIQKRKRHPQQDMIS
MLLKGDKLTEEEAASTCILLAIAGHETTVNLISNSVLCLLQHPEQLLKLR
ENPDLIGTAVEECLRYESPTQMTARVASEDIDICGVTIRQGEQVYLLLGA
ANRDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIAINTL
LQRMPSLNLADEWRYRPLFGFRALEELPVTFE
3D structure
PDB3ejd Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
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) Q166 A234 E237 T238 T239 C344 L345 G346 E353 F383
Catalytic site (residue number reindexed from 1) Q158 A223 E226 T227 T228 C333 L334 G335 E342 F371
Enzyme Commision number 1.14.14.46: pimeloyl-[acyl-carrier protein] 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 ZMQ B Y36 R59 P61 L62 P63 I168 F170 R172 T284 Y306 Y28 R51 P53 L54 P55 I160 F162 R164 T273 Y295
BS02 HEM B M80 L81 H88 R92 L231 A234 T238 T239 P280 T281 T284 R286 S336 F337 H342 C344 M72 L73 H80 R84 L220 A223 T227 T228 P269 T270 T273 R275 S325 F326 H331 C333
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:0009102 biotin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ejd, PDBe:3ejd, PDBj:3ejd
PDBsum3ejd
PubMed18838690
UniProtP53554|BIOI_BACSU Biotin biosynthesis cytochrome P450 (Gene Name=bioI)

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