Structure of PDB 2jjn Chain A Binding Site BS01

Receptor Information
>2jjn Chain A (length=395) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TIDEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLRDT
ATFSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEP
RIRDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGDWS
GALVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLISRL
VLAEVDGRALDDEEAANFSTALLLAGHITTTVLLGNIVRTLDEHPAHWDA
AAEDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNTWV
LSANRDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENRVA
LEEIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain2jjn Chain A Residue 412 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2jjn Investigating the Structural Plasticity of a Cytochrome P450: Three-Dimensional Structures of P450 Eryk and Binding to its Physiological Substrate.
Resolution1.59 Å
Binding residue
(original residue number in PDB)		I87 H88 H95 R99 F106 L238 A241 G242 T245 R293 S345 F346 H351 C353 G355 A359
Binding residue
(residue number reindexed from 1)		I71 H72 H79 R83 F90 L222 A225 G226 T229 R277 S329 F330 H335 C337 G339 A343
Annotation score1
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) D155 A225 I228 T229 T230 C337 L338 G339 E346 V377
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:2jjn, PDBe:2jjn, PDBj:2jjn
PDBsum2jjn
PubMed19625248
UniProtP48635|ERYK_SACEN Erythromycin C-12 hydroxylase (Gene Name=eryK)

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