Structure of PDB 2jjo Chain A Binding Site BS01

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 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 chain2jjo 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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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)		H95 R99 F106 L238 A241 G242 T245 T246 L249 M291 R293 S345 F346 H351 C353 L354 G355 A359
Binding residue
(residue number reindexed from 1)		H77 R81 F88 L220 A223 G224 T227 T228 L231 M273 R275 S327 F328 H333 C335 L336 G337 A341
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) 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

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Molecular Function
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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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