Structure of PDB 3ofu Chain C

Receptor sequence
>3ofuC (length=396) Species: 279238 (Novosphingobium aromaticivorans DSM 12444) [Search protein sequence]
MIPAHVPADRVVDFDIFNPPGVEQDYFAAWKTLLDGPGLVWSTANGGHWI
AARGDVVRELWGDAERLSSQCLAVTPGLGKVMQFIPLQQDGAEHKAFRTP
VMKGLASRFVVALEPKVQAVARKLMESLRPRGSCDFVSDFAEILPLNIFL
TLIDVPLEDRPRLRQLGVQLTRPDGSMTVEQLKQAADDYLWPFIEKRMAQ
PGDDLFSRILSEPVGGRPWTVDEARRMCRNLLFGGLDTVAAMIGMVALHL
ARHPEDQRLLRERPDLIPAAADELMRRYPTVAVSRNAVADVDADGVTIRK
GDLVYLPSVLHNLDPASFEAPEEVRFDRGLAPIRHTTMGVGAHRCVGAGL
ARMEVIVFLREWLGGMPEFALAPDKAVTMKGGNVGACTALPLVWRA
3D structure
PDB3ofu Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.
ChainC
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R172 G234 D237 T238 V239 C345 V346 G347 E354 V384
Catalytic site (residue number reindexed from 1) R172 G234 D237 T238 V239 C345 V346 G347 E354 V384
Enzyme Commision number ?
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 C P86 L87 H94 R98 N230 L231 G234 G235 T238 V239 V283 R285 M338 H343 C345 V346 L350 P86 L87 H94 R98 N230 L231 G234 G235 T238 V239 V283 R285 M338 H343 C345 V346 L350
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:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3ofu, PDBe:3ofu, PDBj:3ofu
PDBsum3ofu
PubMed21154803
UniProtQ2G637

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