Structure of PDB 3eje Chain B

Receptor sequence

>3ejeB (length=378) Species: 1423 (Bacillus subtilis)

SEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDARFKV
RTPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTESYQ
PYIIETVHHLLDQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDREQLK
EWAASLIQTIDFTRSRKALTEGNIMAVQAMAYFKELIQKRKRHPQQDMIS
MLLKKLTEEEAASTCILLAIAGHETTVNLISNSVLCLLQHPEQLLKLREN
PDLIGTAVEECLRYESPTQMTARVASEDIDICGVTIRQGEQVYLLLGAAN
RDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIAINTLLQ
RMPSLNLAWRYRPLFGFRALEELPVTFE

3D structure

• PDB: 3eje Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
• Chain: B
• 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 A221 E224 T225 T226 C331 L332 G333 E340 F367
• 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	ZMO	B	Y36 R59 T60 P61 L62 P63 I168 F170 R172 I233 A234 T281 M283 T284 Q304 Y306	Y28 R51 T52 P53 L54 P55 I160 F162 R164 I220 A221 T268 M270 T271 Q291 Y293
BS02	HEM	B	M80 L81 H88 R92 L231 A234 T238 P280 T284 R286 S336 F337 H342 C344 L345	M72 L73 H80 R84 L218 A221 T225 P267 T271 R273 S323 F324 H329 C331 L332

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