Structure of PDB 6jst Chain A Binding Site BS03

Receptor Information
>6jst Chain A (length=323) Species: 235909 (Geobacillus kaustophilus HTA426) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EMVETVCGPVPVEQLGKTLIHEHFLFGYPGFQGDVTRGTFREDESLRVAV
EAAEKMKRHGIQTVVDPTPNDCGRNPAFLRRVAEETGLNIICATGYPYEG
EGAPPYFQFRRLLGTAEDDIYDMFMAELTEGIADTGIKAGVIKLASSKGR
ITEYEKMFFRAAARAQKETGAVIITHTQEGTMGPEQAAYLLEHGADPKKI
VIGHMCGNTDPDYHRKTLAYGVYIAFDRFGIQGMVGAPTDEERVRTLLAL
LRDGYEKQIMLSHNTVNVWLGRPFTLPEPFAEMMKNWHVEHLFVNIIPAL
KNEGIRDEVLEQMFIGNPAALFS
Ligand information
Ligand IDLAE
InChIInChI=1S/C12H19NO4/c1-2-3-4-5-9(14)8-11(15)13-10-6-7-17-12(10)16/h10H,2-8H2,1H3,(H,13,15)/t10-/m0/s1
InChIKeyFXCMGCFNLNFLSH-JTQLQIEISA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C1OCCC1NC(=O)CC(=O)CCCCC
OpenEye OEToolkits 1.5.0CCCCCC(=O)CC(=O)NC1CCOC1=O
CACTVS 3.341CCCCCC(=O)CC(=O)N[CH]1CCOC1=O
CACTVS 3.341
OpenEye OEToolkits 1.5.0		CCCCCC(=O)CC(=O)N[C@H]1CCOC1=O
FormulaC12 H19 N O4
Name3-OXO-OCTANOIC ACID (2-OXO-TETRAHYDRO-FURAN-3-YL)-AMIDE;
N-(3-OXO-OCTANAL-1-YL)-HOMOSERINE LACTONE
ChEMBLCHEMBL463321
DrugBankDB08081
ZINCZINC000004102231
PDB chain6jst Chain A Residue 404 [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]
PDB6jst Directed Computational Evolution of Quorum-Quenching Lactonases from the Amidohydrolase Superfamily.
Resolution1.726 Å
Binding residue
(original residue number in PDB)		Y30 N266 V268 F276 L278 W289
Binding residue
(residue number reindexed from 1)		Y28 N264 V266 F274 L276 W287
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H23 H25 K145 H178 H206 G209 R230 N266
Catalytic site (residue number reindexed from 1) H21 H23 K143 H176 H204 G207 R228 N264
Enzyme Commision number 3.5.-.-
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6jst, PDBe:6jst, PDBj:6jst
PDBsum6jst
PubMed32320671
UniProtQ5KZU5

[Back to BioLiP]