Structure of PDB 2jjp Chain A

Receptor sequence
>2jjpA (length=397) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence]
LTTIDEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLR
DTATFSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDL
EPRIRDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGD
WSGALVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLIS
RLVLAEVDGRALDDEEAANFSTALLLAGHITTTVLLGNIVRTLDEHPAHW
DAAAEDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNT
WVLSANRDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENR
VALEEIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA
3D structure
PDB2jjp Azole Drugs Trap Cytochrome P450 Eryk in Alternative Conformational States.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D171 A241 I244 T245 T246 C353 L354 G355 E362 V393
Catalytic site (residue number reindexed from 1) D157 A227 I230 T231 T232 C339 L340 G341 E348 V379
Enzyme Commision number 1.14.13.154: erythromycin 12 hydroxylase.
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 I87 H88 H95 R99 A241 T245 L249 R293 S345 F346 G347 H351 C353 G355 I73 H74 H81 R85 A227 T231 L235 R279 S331 F332 G333 H337 C339 G341
BS02 KLN A H88 M174 F288 Q290 Q292 H74 M160 F274 Q276 Q278 MOAD: Kd=1.12uM
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:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0050661 NADP binding
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0033068 macrolide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2jjp, PDBe:2jjp, PDBj:2jjp
PDBsum2jjp
PubMed20845962
UniProtP48635|ERYK_SACEN Erythromycin C-12 hydroxylase (Gene Name=eryK)

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