Structure of PDB 5l1r Chain A

Receptor sequence

>5l1rA (length=397) Species: 29301 (Streptomyces arenae)

TDLPRLPFDNPDIMGIAPQMLALQKEGPIARVGTAGEDAWLVTRYDEVRT
LLADRRLRLSNPNPQPSAKSAARAFMVALMAGDDHETEPARHAQMRSLLI
PRFSTRRLRLMKTRIEHHVDELLDQLAASAPPVDLHRVLSFRLPTMVVCD
LLGVPLADRERFGQWARGTFDQSDNEHSANTFQQVVDYMLELVARKRVEP
GDDILSELIAEKDGALSDADIAHLGNAVLLFGYETTIVRIDLGTLLLLRN
PVQRAQLAEDPGLAPAAVEEILRLGVGGKGSNALIPRYAHGDITVGETVI
RTGDAVMLAIGAANYDDRAFPDGGLFDLTRVRPRSHLAFGHGARHCIGRT
LARIELTAVFERLFRRLPDLRLAVPEESLRWQEHRITGGFDEIPVTF

3D structure

• PDB: 5l1r The Cytochrome P450-Catalyzed Oxidative Rearrangement in the Final Step of Pentalenolactone Biosynthesis: Substrate Structure Determines Mechanism.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D172 F232 E235 T236 T237 S282 C347 I348 G349 E356 T388
• Catalytic site (residue number reindexed from 1): D171 F231 E234 T235 T236 S281 C346 I347 G348 E355 T387
• Enzyme Commision number: 1.14.19.8: pentalenolactone 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	HEM	A	M81 H93 R97 F104 F232 G233 T236 R240 I286 R288 A339 F340 R345 C347 G349 A353	M80 H92 R96 F103 F231 G232 T235 R239 I285 R287 A338 F339 R344 C346 G348 A352

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0005506 iron ion binding
• GO:0016636 oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
• 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:0017000 antibiotic biosynthetic process
• GO:1901780 pentalenolactone biosynthetic process

External links

• PDB: RCSB:5l1r, PDBe:5l1r, PDBj:5l1r
• PDBsum: 5l1r
• PubMed: 27588339
• UniProt: E3VWI3|PNTM_STRAE Pentalenolactone synthase (Gene Name=pntM)