Structure of PDB 2rfc Chain B

Receptor sequence

>2rfcB (length=338)

LNDPVHYDGAWHVYKYSDVKHVLMNDKIFSSNPGNRYSGISFITMDNPEH
KEFRDISAPYFLPSKINDYKDFIEETSNDLIKNIDNKDIISEYAVRLPVN
IISKILGIPDSDMPLFKLWSDYIIGNKRDENFNYVNNRMVSRLLEIFKSD
SHGIINVLAGSSLKNRKLTMDEKIKYIMLLIIGGNETTTNLIGNMIRVID
ENPDIIDDALKNRSGFVEETLRYYSPIQFLPHRFAAEDSYINNKKIKKGD
QVIVYLGSANRDETFFDEPDLFKIGRREMHLAFGIGIHMCLGAPLARLEA
SIALNDILNHFKRIKIDYKKSRLLDNKMVLGYDKLFLS

3D structure

• PDB: 2rfc Crystal Structure and Properties of CYP231A2 from the Thermoacidophilic Archaeon Picrophilus torridus.
• Chain: B
• Resolution: 3.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G139 G197 E200 T201 T202 I241 C304 L305 G306 E313 V343
• Catalytic site (residue number reindexed from 1): G125 G183 E186 T187 T188 I227 C290 L291 G292 E299 V329
• Enzyme Commision number: 1.14.14.1: unspecific monooxygenase.

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	B	R68 L193 L194 G198 T201 T202 L205 L244 R247 A296 F297 H302 C304 G306 A310	R54 L179 L180 G184 T187 T188 L191 L230 R233 A282 F283 H288 C290 G292 A296
BS02	PIM	B	I57 G197 T201	I43 G183 T187

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:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
• GO:0020037 heme binding
• GO:0046872 metal ion binding

External links

• PDB: RCSB:2rfc, PDBe:2rfc, PDBj:2rfc
• PDBsum: 2rfc
• PubMed: 18197710
• UniProt: Q6KZ68