Structure of PDB 2jjo Chain A Binding Site BS02

Receptor Information
>2jjo Chain A (length=393) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLRDTAT
FSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEPRI
RDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGDWSGA
LVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLISRLVL
AEVDGRALDDEEAANFSTALLLAGHITTTVLLGNIVRTLDEHPAHWDAAA
EDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNTWVLS
ANRDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENRVALE
EIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA
Ligand information
Ligand IDEY5
InChIInChI=1S/C36H65NO12/c1-13-25-19(4)28(39)20(5)27(38)17(2)15-36(10,44)32(49-34-29(40)24(37(11)12)14-18(3)45-34)21(6)30(22(7)33(42)47-25)48-26-16-35(9,43)31(41)23(8)46-26/h17-26,28-32,34,39-41,43-44H,13-16H2,1-12H3/t17-,18-,19+,20+,21+,22-,23+,24+,25-,26+,28+,29-,30+,31+,32-,34+,35-,36-/m1/s1
InChIKeyCLQUUOKNEOQBSW-KEGKUKQHSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C3OC(CC)C(C)C(O)C(C(=O)C(C)CC(O)(C)C(OC1OC(C)CC(N(C)C)C1O)C(C(OC2OC(C(O)C(O)(C2)C)C)C3C)C)C
OpenEye OEToolkits 1.5.0CCC1C(C(C(C(=O)C(CC(C(C(C(C(C(=O)O1)C)OC2CC(C(C(O2)C)O)(C)O)C)OC3C(C(CC(O3)C)N(C)C)O)(C)O)C)C)O)C
CACTVS 3.341CC[CH]1OC(=O)[CH](C)[CH](O[CH]2C[C](C)(O)[CH](O)[CH](C)O2)[CH](C)[CH](O[CH]3O[CH](C)C[CH]([CH]3O)N(C)C)[C](C)(O)C[CH](C)C(=O)[CH](C)[CH](O)[CH]1C
CACTVS 3.341CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@H]2C[C@@](C)(O)[C@@H](O)[C@H](C)O2)[C@H](C)[C@@H](O[C@@H]3O[C@H](C)C[C@@H]([C@H]3O)N(C)C)[C@](C)(O)C[C@@H](C)C(=O)[C@H](C)[C@@H](O)[C@H]1C
OpenEye OEToolkits 1.5.0CC[C@@H]1[C@@H]([C@@H]([C@H](C(=O)[C@@H](C[C@@]([C@@H]([C@H]([C@@H]([C@H](C(=O)O1)C)O[C@H]2C[C@@]([C@H]([C@@H](O2)C)O)(C)O)C)O[C@H]3[C@@H]([C@H](C[C@H](O3)C)N(C)C)O)(C)O)C)C)O)C
FormulaC36 H65 N O12
NameErythromycin D
ChEMBL
DrugBank
ZINCZINC000087493168
PDB chain2jjo Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2jjo Investigating the Structural Plasticity of a Cytochrome P450: Three-Dimensional Structures of P450 Eryk and Binding to its Physiological Substrate.
Resolution1.99 Å
Binding residue
(original residue number in PDB)		H88 E89 L169 M174 I186 A237 A241 T245 F288 Q292
Binding residue
(residue number reindexed from 1)		H70 E71 L151 M156 I168 A219 A223 T227 F270 Q274
Annotation score5
Binding affinityMOAD: Kd=3.5uM
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) D153 A223 I226 T227 T228 C335 L336 G337 E344 V375
Enzyme Commision number 1.14.13.154: erythromycin 12 hydroxylase.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2jjo, PDBe:2jjo, PDBj:2jjo
PDBsum2jjo
PubMed19625248
UniProtP48635|ERYK_SACEN Erythromycin C-12 hydroxylase (Gene Name=eryK)

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