Structure of PDB 2acz Chain C Binding Site BS03

Receptor Information
>2acz Chain C (length=129) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGT
SLSSPEGFEQASAIMGSFFVKFIMWGILTALAYHVVVGIRHMMMDFGYLE
ETFEAGKRSAKISFVITVVLSLLAGVLVW
Ligand information
Ligand IDCDN
InChIInChI=1S/C58H120O17P2/c1-5-9-13-16-19-22-25-27-30-33-36-40-44-57(62)74-53(48-68-55(60)42-38-12-8-4)50-72-76(64,65)70-46-52(59)47-71-77(66,67)73-51-54(49-69-56(61)43-39-35-32-29-24-21-18-15-11-7-3)75-58(63)45-41-37-34-31-28-26-23-20-17-14-10-6-2/h52-63H,5-51H2,1-4H3,(H,64,65)(H,66,67)/t52-,53+,54+,55?,56?,57?,58-/m0/s1
InChIKeyGKRASOJOCMJQMF-DUXRJKJQSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCCCCCCCCCCCCC[C@H](O)O[C@H](CO[C@H](O)CCCCC)CO[P@](O)(=O)OC[C@H](O)CO[P@](O)(=O)OC[C@@H](CO[C@H](O)CCCCCCCCCCCC)O[C@H](O)CCCCCCCCCCCCCC
ACDLabs 10.04O=P(O)(OCC(OC(O)CCCCCCCCCCCCCC)COC(O)CCCCC)OCC(O)COP(=O)(OCC(OC(O)CCCCCCCCCCCCCC)COC(O)CCCCCCCCCCCC)O
OpenEye OEToolkits 1.5.0CCCCCCCCCCCCCCC(O)OC(COC(CCCCC)O)COP(=O)(O)OCC(COP(=O)(O)OCC(COC(CCCCCCCCCCCC)O)OC(CCCCCCCCCCCCCC)O)O
OpenEye OEToolkits 1.5.0CCCCCCCCCCCCCCC(O)O[C@H](COC(CCCCC)O)CO[P@@](=O)(O)OC[C@@H](CO[P@@](=O)(O)OC[C@@H](COC(CCCCCCCCCCCC)O)O[C@@H](CCCCCCCCCCCCCC)O)O
CACTVS 3.341CCCCCCCCCCCCCC[CH](O)O[CH](CO[CH](O)CCCCC)CO[P](O)(=O)OC[CH](O)CO[P](O)(=O)OC[CH](CO[CH](O)CCCCCCCCCCCC)O[CH](O)CCCCCCCCCCCCCC
FormulaC58 H120 O17 P2
NameCARDIOLIPIN
ChEMBL
DrugBank
ZINC
PDB chain2acz Chain C Residue 132 [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]
PDB2acz Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		V41 S51 A61 S62 M65 L78 A82 L123 V126 L127 W129
Binding residue
(residue number reindexed from 1)		V41 S51 A61 S62 M65 L78 A82 L123 V126 L127 W129
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0008177 succinate dehydrogenase (quinone) activity
GO:0009055 electron transfer activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0048039 ubiquinone binding
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0009060 aerobic respiration
GO:0017004 cytochrome complex assembly
GO:0019646 aerobic electron transport chain
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2acz, PDBe:2acz, PDBj:2acz
PDBsum2acz
PubMed16407191
UniProtP69054|DHSC_ECOLI Succinate dehydrogenase cytochrome b556 subunit (Gene Name=sdhC)

[Back to BioLiP]