Structure of PDB 2xfh Chain A Binding Site BS01

Receptor Information
>2xfh Chain A (length=394) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IDEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLRDTA
TFSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEPR
IRDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGDWSG
ALVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLISRLV
LAEVDGRALDDEEAANFSTALLLAGHITTTVLLGNIVRTLDEHPAHWDAA
AEDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNTWVL
SANRDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENRVAL
EEIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA
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 chain2xfh Chain A Residue 1412 [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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PDB2xfh Azole Drugs Trap Cytochrome P450 Eryk in Alternative Conformational States.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		I87 H88 H95 R99 F106 L238 A241 T245 L249 P287 F288 M291 R293 S345 F346 H351 C353 G355 A359
Binding residue
(residue number reindexed from 1)		I70 H71 H78 R82 F89 L221 A224 T228 L232 P270 F271 M274 R276 S328 F329 H334 C336 G338 A342
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) D154 A224 I227 T228 T229 C336 L337 G338 E345 V376
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:2xfh, PDBe:2xfh, PDBj:2xfh
PDBsum2xfh
PubMed20845962
UniProtP48635|ERYK_SACEN Erythromycin C-12 hydroxylase (Gene Name=eryK)

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