Structure of PDB 3eje Chain D

Receptor sequence

>3ejeD (length=385) Species: 1423 (Bacillus subtilis)

TASSEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDAR
FKVRTPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTE
SYQPYIIETVHHLLDQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDRE
QLKEWAASLIQTIDFTRSRKALTEGNIMAVQAMAYFKELIQKRKRHPQQD
MISMLLKGRKLTEEEAASTCILLAIAGHETTVNLISNSVLCLLQHPEQLL
KLRENPDLIGTAVEECLRYESPTQMTARVASEDIDICGVTIRQGEQVYLL
LGAANRDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIAI
NTLLQRMPSLNLADFWRYRPLFGFRALEELPVTFE

3D structure

• PDB: 3eje Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
• Chain: D
• 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): Q161 A226 E229 T230 T231 C336 L337 G338 E345 F374
• 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	D	Y36 R59 P61 P63 M79 I165 I168 R172 A234 T284 Y306	Y31 R54 P56 P58 M74 I160 I163 R167 A226 T276 Y298
BS02	HEM	D	M80 L81 H88 R92 F99 L231 T238 L242 T284 R286 S336 F337 H342 C344 L345 G346 A350	M75 L76 H83 R87 F94 L223 T230 L234 T276 R278 S328 F329 H334 C336 L337 G338 A342

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)