Structure of PDB 5u21 Chain A

Receptor sequence
>5u21A (length=361) Species: 197 (Campylobacter jejuni) [Search protein sequence]
HMFFLNLKQINDRFNTEFITKFKEILESGWYILGKQCEKFENNFAKYCGV
KHCIGVANGLDALRLIIKAYDFKENDEIIVPANTYIASILAITDNKCKPI
LIEPDINTYNINPDLIEEKITKKTKAIMVVHLYGQVCDMEKIQLLANKYN
LKIIEDCAQAHGAIYKDKRVGNLGDAAGFSFYPGANLGALGDAGCICTND
DNFASKIRALANYGSHKKYENLYTGLNSRLDEIQAAFLDIKLKYLDEDNN
KRKNIANFYLQNIKNENIILPSNKFDHVWHLFVVKTKLRDELQHYLNNHD
IQTIIHYPIPPHKQKCYKDLNHLKLPITENIHQEVLSLPISPTMKENDFK
KVADILNKWKV
3D structure
PDB5u21 Structural investigation on WlaRG from Campylobacter jejuni: A sugar aminotransferase.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y84 D155 Q158 Y181 A184 Y218 R228
Catalytic site (residue number reindexed from 1) Y85 D156 Q159 Y182 A185 Y219 R229
Enzyme Commision number ?
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 TQP A L6 N57 G58 L59 Y84 A86 D155 A157 Q158 S179 Y181 I303 H305 Y306 L7 N58 G59 L60 Y85 A87 D156 A158 Q159 S180 Y182 I304 H306 Y307
BS02 TQP A G28 W29 Y30 Y212 K217 N226 G29 W30 Y31 Y213 K218 N227
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5u21, PDBe:5u21, PDBj:5u21
PDBsum5u21
PubMed28028852
UniProtQ9ALS9

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