Structure of PDB 5fyf Chain B

Receptor sequence
>5fyfB (length=411) Species: 2743 (Marinobacter nauticus) [Search protein sequence]
FVETPIPDVNTLALEDIDVSNPFLYRQGQWRAYFKRLRDEAPVHYQKNSP
FGPFWSVTRFEDILFVDKSHDLFSAEPQIILGDPPVEMFIAMDPPKHDVQ
RSSVQGVVAPKNLKEMEGLIRSRTGDVLDSLPTDKPFNWVPAVSKELTGR
MLATLLDFPYEERHKLVEWSDRMAGAASATGGEFADENAMFDDAADMARS
FSRLWRDKEARRAAGEEPGFDLISLLQSNKETKDLINRPMEFIGNLTLLI
VGGNDTTRNSMSGGLVAMNEFPREFEKLKAKPELIPNMVSEIIRWQTPLA
YMRRIAKQDVELGGQTIRVVMWYASGNRDERKFDNPDQFIIDRKDARNHM
SFGYGVHRCMGNRLAELQLRILWEEILKRFDNIEVVEEPERVQSNFVRGY
SRLMVKLTPNS
3D structure
PDB5fyf Structure-Guided Redesign of CYP153AM.aqfor the Improved Terminal Hydroxylation of Fatty Acids
ChainB
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G234 G311 D314 T315 T316 C422 M423 G424 Q431 V460
Catalytic site (residue number reindexed from 1) G175 G252 D255 T256 T257 C359 M360 G361 Q368 V397
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 B D122 F148 I149 H156 R160 G311 G312 T315 P357 M361 Y386 S414 F415 H420 C422 G424 A428 D67 F89 I90 H97 R101 G252 G253 T256 P298 M302 Y323 S351 F352 H357 C359 G361 A365
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:5fyf, PDBe:5fyf, PDBj:5fyf
PDBsum5fyf
PubMed
UniProtA1TY82

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