Structure of PDB 1oxa Chain A Binding Site BS01

Receptor Information
>1oxa Chain A (length=403) Species: 1836 (Saccharopolyspora erythraea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATVPDLESDSFHVDWYSTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAA
LSDLRLSSDPKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRL
RKLVSQEFTVRRVEAMRPRVEQITAELLDEVGDSGVVDIVDRFAHPLPIK
VICELLGVDEAARGAFGRWSSEILVMDPERAEQRGQAAREVVNFILDLVE
RRRTEPGDDLLSALISVQDDDDGRLSADELTSIALVLLLAGFEASVSLIG
IGTYLLLTHPDQLALVRADPSALPNAVEEILRYIAPPETTTRFAAEEVEI
GGVAIPQYSTVLVANGAANRDPSQFPDPHRFDVTRDTRGHLSFGQGIHFC
MGRPLAKLEGEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVR
LDG
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 chain1oxa Chain A Residue 410 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1oxa Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		M90 G91 H98 R102 F109 A245 P288 R293 S343 F344 H349 C351 G353
Binding residue
(residue number reindexed from 1)		M89 G90 H97 R101 F108 A244 P287 R292 S342 F343 H348 C350 G352
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V176 A241 E244 A245 S246 C351 M352 G353 E360 L392
Catalytic site (residue number reindexed from 1) V175 A240 E243 A244 S245 C350 M351 G352 E359 L391
Enzyme Commision number 1.14.15.35: 6-deoxyerythronolide B 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:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:1901115 erythromycin biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1oxa, PDBe:1oxa, PDBj:1oxa
PDBsum1oxa
PubMed7749919
UniProtQ00441|CPXJ_SACEN 6-deoxyerythronolide B hydroxylase (Gene Name=eryF)

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