Structure of PDB 1nu1 Chain C Binding Site BS03

Receptor Information
>1nu1 Chain C (length=378) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFL
AMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRG
LYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFWGATVITNLLS
AIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIMAIAMVHLLFLH
ETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALMLLVLFAPDLLG
DPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILIL
ALIPLLHTSKQRSMMFRPLSQCLFWALVADLLTLTWIGGQPVEHPYITIG
QLASVLYFLLILVLMPTAGTIENKLLKW
Ligand information
Ligand IDQNO
InChIInChI=1S/C18H25NO2/c1-2-3-4-5-6-7-8-11-15-14-18(20)16-12-9-10-13-17(16)19(15)21/h9-10,12-14,20H,2-8,11H2,1H3
InChIKeyLMBFBUICIQJLPK-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CCCCCCCCCc1cc(c2ccccc2[n+]1[O-])O
ACDLabs 10.04[O-][n+]2c1ccccc1c(O)cc2CCCCCCCCC
CACTVS 3.341CCCCCCCCCc1cc(O)c2ccccc2[n+]1[O-]
FormulaC18 H25 N O2
Name2-NONYL-4-HYDROXYQUINOLINE N-OXIDE
ChEMBLCHEMBL1235570
DrugBankDB08453
ZINCZINC000100036761
PDB chain1nu1 Chain C Residue 383 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1nu1 Structural basis for the quinone reduction in the bc(1) complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc(1) with bound substrate and inhibitors at the Q(i) site
Resolution3.2 Å
Binding residue
(original residue number in PDB)		F18 I27 S35 F220 Y224 D228
Binding residue
(residue number reindexed from 1)		F17 I26 S34 F219 Y223 D227
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.19,Kd=64nM
Enzymatic activity
Catalytic site (original residue number in PDB) H201 S205 K227 D228 E271
Catalytic site (residue number reindexed from 1) H200 S204 K226 D227 E270
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0008121 ubiquinol-cytochrome-c reductase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0048039 ubiquinone binding
Biological Process
GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c
GO:0022904 respiratory electron transport chain
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0016020 membrane
GO:0031966 mitochondrial membrane
GO:0045275 respiratory chain complex III

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1nu1, PDBe:1nu1, PDBj:1nu1
PDBsum1nu1
PubMed12885240
UniProtP00157|CYB_BOVIN Cytochrome b (Gene Name=MT-CYB)

[Back to BioLiP]