Structure of PDB 2xfh Chain A Binding Site BS02

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 IDCL6
InChIInChI=1S/C22H17ClN2/c23-21-14-8-7-13-20(21)22(25-16-15-24-17-25,18-9-3-1-4-10-18)19-11-5-2-6-12-19/h1-17H
InChIKeyVNFPBHJOKIVQEB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(cc1)C(c2ccccc2)(c3ccccc3Cl)n4ccnc4
ACDLabs 10.04Clc1ccccc1C(c2ccccc2)(c3ccccc3)n4ccnc4
CACTVS 3.341Clc1ccccc1C(n2ccnc2)(c3ccccc3)c4ccccc4
FormulaC22 H17 Cl N2
Name1-[(2-CHLOROPHENYL)(DIPHENYL)METHYL]-1H-IMIDAZOLE;
CLOTRIMAZOLE
ChEMBLCHEMBL104
DrugBankDB00257
ZINCZINC000003807804
PDB chain2xfh Chain A Residue 1413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		H88 A237 A241 F288
Binding residue
(residue number reindexed from 1)		H71 A220 A224 F271
Annotation score1
Binding affinityMOAD: Kd<0.01uM
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

View graph for
Molecular Function
View graph for
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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