Structure of PDB 3nu7 Chain A

Receptor sequence
>3nu7A (length=358) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
IEFIDLKNQQARIKDKIDAGIQRVLRHGQYILGPEVTELEDRLADFVGAK
YCISCANGTDALQIVQMALGVGPGDEVITPGFTYVATAETVALLGAKPVY
VDIDPRTYNLDPQLLEAAITPRTKAIIPVSLYGQCADFDAINAIASKYGI
PVIEDAAQSFGASYKGKRSCNLSTVACTSFFPSKPLGCYGDGGAIFTNDD
ELATAIRQIARHGQDRRYHHIRVGVNSRLDTLQAAILLPKLEIFEEEIAL
RQKVAAEYDLSLKQVGIGTPFIEVNNISVYAQYTVRMDNRESVQASLKAA
GVPTAVHYPIPLNKQPAVADEKAKLPVGDKAATQVMSLPMHPYLDTASIK
IICAALTN
3D structure
PDB3nu7 Structural Analysis of WbpE from Pseudomonas aeruginosa PAO1: A Nucleotide Sugar Aminotransferase Involved in O-Antigen Assembly
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y85 D156 Q159 F182 K185 Y219 R229
Catalytic site (residue number reindexed from 1) Y84 D155 Q158 F181 K184 Y218 R228
Enzyme Commision number 2.6.1.98: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase.
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 PMP A N58 G59 T60 Y85 A87 D156 A158 Q159 S180 K185 N57 G58 T59 Y84 A86 D155 A157 Q158 S179 K184
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009243 O antigen biosynthetic process
GO:0071555 cell wall organization

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3nu7, PDBe:3nu7, PDBj:3nu7
PDBsum3nu7
PubMed20604544
UniProtQ9HZ76|WBPE_PSEAE UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase (Gene Name=wbpE)

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