Structure of PDB 1o69 Chain B

Receptor sequence
>1o69B (length=368) Species: 197 (Campylobacter jejuni) [Search protein sequence]
GNELKYIEEVFKSGEFVNRFEQSVKDYSKSENALALNSATAALHLALRVA
GVKQDDIVLASSFTFIASVAPICYLKAKPVFIDCDETYNIDVDLLKLAIK
ECEKKPKALILTHLYGNAAKMDEIVEICKENDIVLIEDAAEALGSFYKNK
ALGTFGEFGVYSYNGNKIITTSGGGMLIGKNKEKIEKARFYSTQARENCL
HYEHLDYGYNYRLSNVLGAIGVAQMEVLEQRVLKKREIYEWYKEFLGEYF
SFLDELENSRSNRWLSTALINFDKNELNACQKDINISQKNITLHPKISKL
IEDLKNKQIETRPLWKAMHTQEVFKGAKAYLNGNSELFFQKGICLPSGTA
MSKDDVYEISKLILKSIK
3D structure
PDB1o69 Structural analysis of a set of proteins resulting from a bacterial genomics project
ChainB
Resolution1.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 X04 B S55 A56 T57 F82 S85 D155 A157 E158 S179 N183 S38 A39 T40 F65 S68 D138 A140 E141 S162 N166
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

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

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