Structure of PDB 2bpo Chain A Binding Site BS02

Receptor Information
>2bpo Chain A (length=641) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NRDIAQVVTENNKNYLVLYASQTGTAEGFAKAFSKELVAKFNLNVMCADV
ENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLR
YNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDY
MAWKDSILEVLKDELHLDEQEAKFTSQFQYTVLNEITDSMSLGEPSAHYL
PSHQLNRNADGIQLGPFDLSQPYIAPIVKSRELFSSNDRNCIHSEFDLSG
SNIKYSTGDHLAVWPSNPLEKVEQFLSIFNLDPETIFDLKPLDPTVKVPF
PTPTTIGAAIKHYLEITGPVSRQLFSSLIQFAPNADVKEKLTLLSKDKDQ
FAVEITSKYFNIADALKYLSDGAKWDTVPMQFLVESVPQMTPRYYSISSS
SLSEKQTVHVTSIVENFPNPELPDAPPVVGVTTNLLRNIQLAQNNVNIAE
TNLPVHYDLNGPRKLFANYKLPVHVRRSNFRLPSNPSTPVIMIGPGTGVA
PFRGFIRERVAFLESQKNVSLGKHILFYGSRNTDDFLYQDEWPEYAKKLD
GSFEMVVAHSRLPNTKKVYVQDKLKDYEDQVFEMINNGAFIYVCGDAKGM
AKGVSTALVGILSRGKSITTDEATELIKMLKTSGRYQEDVW
Ligand information
Ligand IDFMN
InChIInChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
InChIKeyFVTCRASFADXXNN-SCRDCRAPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)O)O)O)O
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
ACDLabs 12.01N=2C(=O)NC(=O)C3=Nc1cc(C)c(C)cc1N(C=23)CC(O)C(O)C(O)COP(=O)(O)O
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c2cc1C
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c2cc1C
FormulaC17 H21 N4 O9 P
NameFLAVIN MONONUCLEOTIDE;
RIBOFLAVIN MONOPHOSPHATE
ChEMBLCHEMBL1201794
DrugBankDB03247
ZINCZINC000003831425
PDB chain2bpo Chain A Residue 751 [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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PDB2bpo Crystal Structure of the Yeast Cpr Triple Mutant: D74G, Y75F, K78A.
Resolution2.9 Å
Binding residue
(original residue number in PDB)
S67 T69 G70 T71 A72 S116 T117 Y118 L152 G153 N154 Y157 F160 V690
Binding residue
(residue number reindexed from 1)
S21 T23 G24 T25 A26 S70 T71 Y72 L106 G107 N108 Y111 F114 V640
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y441 S442 C644 D689 W691
Catalytic site (residue number reindexed from 1) Y395 S396 C594 D639 W641
Enzyme Commision number 1.6.2.4: NADPH--hemoprotein reductase.
Gene Ontology
Molecular Function
GO:0003958 NADPH-hemoprotein reductase activity
GO:0003959 NADPH dehydrogenase activity
GO:0009055 electron transfer activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding
Biological Process
GO:0006696 ergosterol biosynthetic process
GO:0016126 sterol biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2bpo, PDBe:2bpo, PDBj:2bpo
PDBsum2bpo
PubMed
UniProtP16603|NCPR_YEAST NADPH--cytochrome P450 reductase (Gene Name=NCP1)

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