Structure of PDB 1o69 Chain B Binding Site BS01

Receptor Information
>1o69 Chain B (length=368) Species: 197 (Campylobacter jejuni) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GNELKYIEEVFKSGEFVNRFEQSVKDYSKSENALALNSATAALHLALRVA
GVKQDDIVLASSFTFIASVAPICYLKAKPVFIDCDETYNIDVDLLKLAIK
ECEKKPKALILTHLYGNAAKMDEIVEICKENDIVLIEDAAEALGSFYKNK
ALGTFGEFGVYSYNGNKIITTSGGGMLIGKNKEKIEKARFYSTQARENCL
HYEHLDYGYNYRLSNVLGAIGVAQMEVLEQRVLKKREIYEWYKEFLGEYF
SFLDELENSRSNRWLSTALINFDKNELNACQKDINISQKNITLHPKISKL
IEDLKNKQIETRPLWKAMHTQEVFKGAKAYLNGNSELFFQKGICLPSGTA
MSKDDVYEISKLILKSIK
Ligand information
Ligand IDX04
InChIInChI=1S/C8H11N2O6P/c1-4-7(12)5(2-11)6(8(9)10-4)3-16-17(13,14)15/h2,12H,3H2,1H3,(H2,9,10)(H2,13,14,15)
InChIKeyXHTUTGLXZYJZRY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1c(c(c(c(n1)N)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=Cc1c(O)c(nc(N)c1COP(=O)(O)O)C
CACTVS 3.341Cc1nc(N)c(CO[P](O)(O)=O)c(C=O)c1O
FormulaC8 H11 N2 O6 P
Name(2-AMINO-4-FORMYL-5-HYDROXY-6-METHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE;
6-AMINO-PYRIDOXAL-5'-PHOSPHATE
ChEMBL
DrugBank
ZINCZINC000033821556
PDB chain1o69 Chain B Residue 395 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1o69 Structural analysis of a set of proteins resulting from a bacterial genomics project
Resolution1.84 Å
Binding residue
(original residue number in PDB)		S55 A56 T57 F82 S85 D155 A157 E158 S179 N183
Binding residue
(residue number reindexed from 1)		S38 A39 T40 F65 S68 D138 A140 E141 S162 N166
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F82 D155 E158 N181 K184 Y219 R229
Catalytic site (residue number reindexed from 1) F65 D138 E141 N164 K167 Y202 R212
Enzyme Commision number 2.6.1.34: UDP-N-acetylbacillosamine transaminase.
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0047302 UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase activity
Biological Process
GO:0000271 polysaccharide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1o69, PDBe:1o69, PDBj:1o69
PDBsum1o69
PubMed16021622
UniProtQ9S5Y7

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