Structure of PDB 2rfb Chain B

Receptor sequence
>2rfbB (length=335) [Search protein sequence]
MRLNDPVHYDGAWHVYKYSDVKHVLMNDKIFSSNGGISFITMDNPEHKEF
RDISAPYFLPSKINDYKDFIEETSNDLIKNIDNKDIISEYAVRLPVNIIS
KILGIPDSDMPLFKLWSDYIIGNKRDENFNYVNNRMVSRLLEIFKSDSHG
IINVLAGSSLKNRKLTMDEKIKYIMLLIIGGNETTTNLIGNMIRVIDENP
DIIDDALKNRSGFVEETLRYYSPIQFLPHRFAAEDSYINNKKIKKGDQVI
VYLGSANRDETFFDEPDLFKIGRREMHLAFGIGIHMCLGAPLARLEASIA
LNDILNHFKRIKIDYKKSRLLDNKMVLGYDKLFLS
3D structure
PDB2rfb Crystal Structure and Properties of CYP231A2 from the Thermoacidophilic Archaeon Picrophilus torridus.
ChainB
Resolution2.5 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) G122 G180 E183 T184 T185 I224 C287 L288 G289 E296 V326
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 F56 I57 H64 R68 L193 L194 G197 G198 T201 R247 A296 F297 H302 C304 G306 F39 I40 H47 R51 L176 L177 G180 G181 T184 R230 A279 F280 H285 C287 G289
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:2rfb, PDBe:2rfb, PDBj:2rfb
PDBsum2rfb
PubMed18197710
UniProtQ6KZ68

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