Structure of PDB 6bdo Chain B Binding Site BS02

Receptor Information
>6bdo Chain B (length=394) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPSIVILGAGYGGIVAALGLQKRLNYNEADITLVNKNDYHYITTELHQPA
AGTMHHDQARVGIKELIDEKKIKFVKDTVVAIDREQQKVTLQNGELHYDY
LVVGLGSEPETFGIEGLREHAFSINSINSVRIIRQHIEYQFAKFAAEPER
TDYLTIVVGGAGFTGIEFVGELADRMPELCAEYDVDPKLVRIINVEAAPT
VLPGFDPALVNYAMDVLGGKGVEFKIGTPIKRCTPEGVVIEVDGEEEEIK
AATVVWTGGVRGNSIVEKSGFETMRGRIKVDPYLRAPGHENIFIVGDCAL
IINEENNRPYPPTAQIAIQHGENVAANLAALIRGGSMTPFKPHIRGTVAS
LGRNDAIGIVGGRKVYGHAASWLKKLIDMRYLYLIGGLSLVLKK
Ligand information
Ligand IDHQO
InChIInChI=1S/C16H21NO2/c1-2-3-4-5-6-9-13-12-16(18)14-10-7-8-11-15(14)17(13)19/h7-8,10-12,18H,2-6,9H2,1H3
InChIKeyNZPACTGCRWDXCJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]
OpenEye OEToolkits 1.5.0CCCCCCCc1cc(c2ccccc2[n+]1[O-])O
ACDLabs 10.04[O-][n+]2c1ccccc1c(O)cc2CCCCCCC
FormulaC16 H21 N O2
Name2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE;
2-HEPTYL-1-OXY-QUINOLIN-4-OL
ChEMBLCHEMBL1233401
DrugBankDB07918
ZINCZINC000001529909
PDB chain6bdo Chain B Residue 602 [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]
PDB6bdo Structure of the NDH-2 - HQNO inhibited complex provides molecular insight into quinone-binding site inhibitors.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		Q317 I320 G348 I379
Binding residue
(residue number reindexed from 1)		Q315 I318 G346 I377
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) N127 F170 G206 V350 L353 K377
Catalytic site (residue number reindexed from 1) N125 F168 G204 V348 L351 K375
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0019646 aerobic electron transport chain

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6bdo, PDBe:6bdo, PDBj:6bdo
PDBsum6bdo
PubMed29621505
UniProtF5L3B8

[Back to BioLiP]