Structure of PDB 3ejd Chain D

Receptor sequence

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

TASSEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDAR
FKVRTPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTE
SYQPYIIETVHHLLDQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDRE
QLKEWAASLIQTIDFTRSRKALTEGNIMAVQAMAYFKELIQKRKRHPQQD
MISMLLKGREKLTEEEAASTCILLAIAGHETTVNLISNSVLCLLQHPEQL
LKLRENPDLIGTAVEECLRYESPTQMTARVASEDIDICGVTIRQGEQVYL
LLGAANRDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIA
INTLLQRMPSLNLADWRYRPLFGFRALEELPVTFE

3D structure

• PDB: 3ejd 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 A227 E230 T231 T232 C337 L338 G339 E346 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	ZMQ	D	Y36 R59 P61 P63 I168 F170 R172 I233 T284 Y306	Y31 R54 P56 P58 I163 F165 R167 I226 T277 Y299
BS02	HEM	D	M80 L81 H88 R92 F99 L231 A234 T238 L242 T284 R286 S336 F337 G338 H342 C344 L345 G346 A350	M75 L76 H83 R87 F94 L224 A227 T231 L235 T277 R279 S329 F330 G331 H335 C337 L338 G339 A343

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)