Structure of PDB 4l0e Chain A Binding Site BS01

Receptor Information
>4l0e Chain A (length=440) Species: 1001349 (Streptomyces sp. Acta 2897) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSSHHHHHHSSGLVPRGSHSGHMTAHTLPIPDDISTINLTDPRTYEVNDL
SEYWRQLRTTRPLYWHPPVGDAPGFWVVSRYADVMALYKDNKKLTSEKGN
VLVTLLAGGDSAAGKMLAVTDGAMHRGLRNVLLKSFSPQALKPIVDQIRV
NTTRLVVDAARRGECDFAADVAEQIPLNTISDLLGVPAADREFLLKLNKS
ALSSEDQSATDAWLARNEILLYFSELVAERRAKPTEDVISVLANSMVDGK
PLTEEVIVLNCYSLILGGDETSRLSMIDSVQTFTQYPDQWELLRDGKVTL
ESATEEVLRWATPAMHFGRRAVTDMELHGQVIAAGDVVTLWNNSANRDEE
VFADPYAFDLNRSPNKHITFGYGPHFCLGAYLGRAEVHALLDALRTYTTG
FEITGEPQRIHSNFLTGLSRLPVRIQPNEAAIAAYDSDNG
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 chain4l0e Chain A Residue 501 [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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PDB4l0e Cytochrome p450sky interacts directly with the nonribosomal Peptide synthetase to generate three amino Acid precursors in skyllamycin biosynthesis.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		Y66 L95 A96 H103 R107 I158 L244 G247 G248 T251 F297 R299 T349 F350 G351 H355 C357 L358 G359
Binding residue
(residue number reindexed from 1)		Y88 L117 A118 H125 R129 I180 L264 G267 G268 T271 F317 R319 T369 F370 G371 H375 C377 L378 G379
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S181 G247 E250 T251 S252 C357 L358 G359 E366 L395
Catalytic site (residue number reindexed from 1) S203 G267 E270 T271 S272 C377 L378 G379 E386 L415
Enzyme Commision number 1.14.-.-
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0036199 cholest-4-en-3-one 26-monooxygenase activity
GO:0046872 metal ion binding
Biological Process
GO:0006707 cholesterol catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4l0e, PDBe:4l0e, PDBj:4l0e
PDBsum4l0e
PubMed24079328
UniProtF2YRY7

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