Structure of PDB 3ejd Chain F

Receptor sequence

>3ejdF (length=381) Species: 1423 (Bacillus subtilis)

SEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDARFKV
RTPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTESYQ
PYIIETVHHLLDQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDREQLK
EWAASLIQTIDFTRSRKALTEGNIMAVQAMAYFKELIQKRKRHPQQDMIS
MLLKGRDKLTEEEAASTCILLAIAGHETTVNLISNSVLCLLQHPEQLLKL
RENPDLIGTAVEECLRYESPTQMTARVASEDIDICGVTIRQGEQVYLLLG
AANRDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIAINT
LLQRMPSLNLAWRYRPLFGFRALEELPVTFE

3D structure

• PDB: 3ejd Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
• Chain: F
• Resolution: 2.1 Å

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 A224 E227 T228 T229 C334 L335 G336 E343 F370
• 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	F	Y36 R59 P61 L62 P63 I168 F170 R172 A234 T281 T284 Y306	Y28 R51 P53 L54 P55 I160 F162 R164 A224 T271 T274 Y296
BS02	HEM	F	M80 L81 H88 R92 L231 A234 T238 L242 T284 R286 S336 F337 G338 H342 C344 L345 A350	M72 L73 H80 R84 L221 A224 T228 L232 T274 R276 S326 F327 G328 H332 C334 L335 A340

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

External links

• PDB: RCSB:3ejd, PDBe:3ejd, PDBj:3ejd
• PDBsum: 3ejd
• PubMed: 18838690
• UniProt: P53554|BIOI_BACSU Biotin biosynthesis cytochrome P450 (Gene Name=bioI)