Structure of PDB 4l0e Chain A

Receptor sequence

>4l0eA (length=440) Species: 1001349 (Streptomyces sp. Acta 2897)

GSSHHHHHHSSGLVPRGSHSGHMTAHTLPIPDDISTINLTDPRTYEVNDL
SEYWRQLRTTRPLYWHPPVGDAPGFWVVSRYADVMALYKDNKKLTSEKGN
VLVTLLAGGDSAAGKMLAVTDGAMHRGLRNVLLKSFSPQALKPIVDQIRV
NTTRLVVDAARRGECDFAADVAEQIPLNTISDLLGVPAADREFLLKLNKS
ALSSEDQSATDAWLARNEILLYFSELVAERRAKPTEDVISVLANSMVDGK
PLTEEVIVLNCYSLILGGDETSRLSMIDSVQTFTQYPDQWELLRDGKVTL
ESATEEVLRWATPAMHFGRRAVTDMELHGQVIAAGDVVTLWNNSANRDEE
VFADPYAFDLNRSPNKHITFGYGPHFCLGAYLGRAEVHALLDALRTYTTG
FEITGEPQRIHSNFLTGLSRLPVRIQPNEAAIAAYDSDNG

3D structure

• PDB: 4l0e Cytochrome p450sky interacts directly with the nonribosomal Peptide synthetase to generate three amino Acid precursors in skyllamycin biosynthesis.
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S181 G247 E250 T251 S252 C357 L358 G359 E366 L395
• Catalytic site (residue number reindexed from 1): S203 G267 E270 T271 S272 C377 L378 G379 E386 L415
• Enzyme Commision number: 1.14.-.-

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	HEM	A	Y66 L95 A96 H103 R107 I158 L244 G247 G248 T251 F297 R299 T349 F350 G351 H355 C357 L358 G359	Y88 L117 A118 H125 R129 I180 L264 G267 G268 T271 F317 R319 T369 F370 G371 H375 C377 L378 G379

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0005506 iron ion binding
• GO:0008395 steroid hydroxylase activity
• GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
• GO:0020037 heme binding
• GO:0036199 cholest-4-en-3-one 26-monooxygenase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006707 cholesterol catabolic process

External links

• PDB: RCSB:4l0e, PDBe:4l0e, PDBj:4l0e
• PDBsum: 4l0e
• PubMed: 24079328
• UniProt: F2YRY7