Structure of PDB 2rfc Chain D

Receptor sequence

>2rfcD (length=338) [Search protein sequence]

LNDPVHYDGAWHVYKYSDVKHVLMNDKIFSSNPGNRYSGISFITMDNPEH
KEFRDISAPYFLPSKINDYKDFIEETSNDLIKNIDNKDIISEYAVRLPVN
IISKILGIPDSDMPLFKLWSDYIIGNKRDENFNYVNNRMVSRLLEIFKSD
SHGIINVLAGSSLKNRKLTMDEKIKYIMLLIIGGNETTTNLIGNMIRVID
ENPDIIDDALKNRSGFVEETLRYYSPIQFLPHRFAAEDSYINNKKIKKGD
QVIVYLGSANRDETFFDEPDLFKIGRREMHLAFGIGIHMCLGAPLARLEA
SIALNDILNHFKRIKIDYKKSRLLDNKMVLGYDKLFLS

3D structure

PDB

2rfc Crystal Structure and Properties of CYP231A2 from the Thermoacidophilic Archaeon Picrophilus torridus.

Chain

Resolution

3.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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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	D	F56 I57 H64 R68 L194 G197 G198 T201 L244 R247 F297 H302 C304 G306	F42 I43 H50 R54 L180 G183 G184 T187 L230 R233 F283 H288 C290 G292
BS02	PIM	D	I196 G197 T201	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

View graph for
Molecular Function

External links

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

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