Structure of PDB 6bfh Chain A Binding Site BS01

Receptor Information
>6bfh Chain A (length=176) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EKKRVSFRPMNEDDLVLMLKWLTDDRVLEFYDGRDKKHTQKTIREHYTEQ
WADEIYRVIIEYDTIPIGYAQIYRIQGELFDEYNYHETEEKIYAMDQFIG
EPEYWNMGIGAEYCRVVCQYLRTEMDADAVILDPRKNNLRAVRAYQKAGF
KIIKELPEHELHEGKKEDCVLMEWRV
Ligand information
Ligand IDKAN
InChIInChI=1S/C18H36N4O11/c19-2-6-10(25)12(27)13(28)18(30-6)33-16-5(21)1-4(20)15(14(16)29)32-17-11(26)8(22)9(24)7(3-23)31-17/h4-18,23-29H,1-3,19-22H2/t4-,5+,6-,7-,8+,9-,10-,11-,12+,13-,14-,15+,16-,17-,18-/m1/s1
InChIKeySBUJHOSQTJFQJX-NOAMYHISSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC[CH]1O[CH](O[CH]2[CH](N)C[CH](N)[CH](O[CH]3O[CH](CO)[CH](O)[CH](N)[CH]3O)[CH]2O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H](O[C@H]3O[C@H](CO)[C@@H](O)[C@H](N)[C@H]3O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04O(C2C(O)C(OC1OC(CN)C(O)C(O)C1O)C(N)CC2N)C3OC(C(O)C(N)C3O)CO
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CN)O)O)O)O)O[C@@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)N)O)N
OpenEye OEToolkits 1.5.0C1C(C(C(C(C1N)OC2C(C(C(C(O2)CN)O)O)O)O)OC3C(C(C(C(O3)CO)O)N)O)N
FormulaC18 H36 N4 O11
NameKANAMYCIN A
ChEMBLCHEMBL1384
DrugBankDB01172
ZINCZINC000008214590
PDB chain6bfh Chain A Residue 201 [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]
PDB6bfh Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6')-Im.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		Y33 D34 W53 E84 Y85 D98 D135
Binding residue
(residue number reindexed from 1)		Y31 D32 W51 E82 Y83 D96 D133
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0016410 N-acyltransferase activity
GO:0016740 transferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
Biological Process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6bfh, PDBe:6bfh, PDBj:6bfh
PDBsum6bfh
PubMed29234669
UniProtQ93ET8

[Back to BioLiP]