Structure of PDB 2d0e Chain A Binding Site BS02

Receptor Information
>2d0e Chain A (length=404) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ETISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWL
VTRHDDVRLVTNDPRFGREAVMDRQVTRLAPHFIPARGAVGFLDPPDHTR
LRRSVAAAFTARGVERVRERSRGMLDELVDAMLRAGPPADLTEAVLSPFP
IAVICELMGVPATDRHSMHTWTQLILSSSHGAEVSERAKNEMNAYFSDLI
GLRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQIGGEAVTNNSGQM
FHLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALEDVEI
KGVRIRAGDAVYVSYLAANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYC
PGGMLARLESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEALPVT
WHHA
Ligand information
Ligand IDNQ
InChIInChI=1S/C10H6O3/c11-8-5-9(12)10(13)7-4-2-1-3-6(7)8/h1-5,12H
InChIKeyCSFWPUWCSPOLJW-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC1=CC(=O)c2ccccc2C1=O
ACDLabs 10.04O=C2c1c(cccc1)C(=O)C(O)=C2
OpenEye OEToolkits 1.5.0c1ccc2c(c1)C(=O)C=C(C2=O)O
FormulaC10 H6 O3
Name2-HYDROXYNAPHTHOQUINONE;
2-HYDROXY-1,4-NAPHTHOQUINONE
ChEMBLCHEMBL240963
DrugBankDB04744
ZINCZINC000004632115
PDB chain2d0e Chain A Residue 409 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2d0e Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer
Resolution2.15 Å
Binding residue
(original residue number in PDB)		L238 H287 R288 I394
Binding residue
(residue number reindexed from 1)		L235 H284 R285 I391
Annotation score2
Binding affinityMOAD: Kd=43uM
Enzymatic activity
Catalytic site (original residue number in PDB) S180 G242 E244 A245 V246 N289 C353 P354 G355 E362 I394
Catalytic site (residue number reindexed from 1) S177 G239 E241 A242 V243 N286 C350 P351 G352 E359 I391
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:2d0e, PDBe:2d0e, PDBj:2d0e
PDBsum2d0e
PubMed16239228
UniProtQ9FCA6|C1582_STRCO Biflaviolin synthase CYP158A2 (Gene Name=cyp158a2)

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