Structure of PDB 2dkk Chain A Binding Site BS01

Receptor Information
>2dkk Chain A (length=399) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPPVRDWPALDLDGPEFDPVLAELMREGPLTRVRLPHGEGWAWLATRYDD
VKAITNDPRFGRAEVTQRQITRLAPHFKPRPGSLAFADQPDHNRLRRAVA
GAFTVGATKRLRPRAQEILDGLVDGILAEGPPADLVERVLEPFPIAVVSE
VMGVPAADRERVHSWTRQIISTSGGAEAAERAKRGLYGWITETVRARAGS
EGGDVYSMLGAAVGRGEVGETEAVGLAGPLQIGGEAVTHNVGQMLYLLLT
RRELMARMRERPGARGTALDELLRWISHRTSVGLARIALEDVEVHGTRIA
AGEPVYVSYLAANRDPDVFPDPDRIDLDRDPNPHLAYGNGHHFCTGAVLA
RMQTELLVDTLLERLPGLRLAVPAEQVAWRRKTMIRGPRTLPCTWHHHH
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 chain2dkk Chain A Residue 430 [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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PDB2dkk Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2.
Resolution1.97 Å
Binding residue
(original residue number in PDB)		R74 L96 A97 H104 F115 G245 A248 H290 Y321 A348 Y349 H354 C356 T357 G358 A362
Binding residue
(residue number reindexed from 1)		R62 L84 A85 H92 F103 G233 A236 H278 Y309 A336 Y337 H342 C344 T345 G346 A350
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S183 G245 E247 A248 V249 T292 C356 T357 G358 Q365 I397
Catalytic site (residue number reindexed from 1) S171 G233 E235 A236 V237 T280 C344 T345 G346 Q353 I385
Enzyme Commision number 1.14.19.69: biflaviolin synthase.
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:0042440 pigment metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2dkk, PDBe:2dkk, PDBj:2dkk
PDBsum2dkk
PubMed17614370
UniProtQ9KZF5|C1581_STRCO Biflaviolin synthase CYP158A1 (Gene Name=cyp158a1)

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