Structure of PDB 2rfc Chain A

Receptor sequence

>2rfcA (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: A
• 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	A	F56 H64 G197 G198 T201 T202 L244 R247 F297 H302 C304 G306	F42 H50 G183 G184 T187 T188 L230 R233 F283 H288 C290 G292
BS02	PIM	A	G53 I196 G197 T201	G39 I182 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