Structure of PDB 3rue Chain b

Receptor sequence
>3rueb (length=336) Species: 703 (Plesiomonas shigelloides) [Search protein sequence]
YMSRYEEITQQLIFSPKTWLITGVAGFIGSNLLEKLLKLNQVVIGLDNFS
TGHQYNLDEVKTLVSTEQWSRFCFIEGDIRDLTTCEQVMKGVDHVLHQAA
LGSVPRSIVDPITTNATNITGFLNILHAAKNAQVQSFTYAASSSTYGDHP
ALPKVEENIGNPLSPYAVTKYVNEIYAQVYARTYGFKTIGLRYFNVFGRR
QDPNGAYAAVIPKWTAAMLKGDDVYINGDGETSRDFCYIDNVIQMNILSA
LAKDSAKDNIYNVAVGDRTTLNELSGYIYDELNLIHHIKYREFRSGDVRH
SQADVTKAIDLLKYRPNIKIREGLRLSMPWYVRFLK
3D structure
PDB3rue Alternative analogs as viable substrates of UDP-hexose 4-epimerases
Chainb
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S143 S144 K170
Catalytic site (residue number reindexed from 1) S143 S144 K170
Enzyme Commision number 5.1.3.7: UDP-N-acetylglucosamine 4-epimerase.
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 NAD b G23 G26 F27 I28 N48 S50 T51 G52 D78 I79 Q98 A99 A100 T117 A140 K170 Y193 V196 G23 G26 F27 I28 N48 S50 T51 G52 D78 I79 Q98 A99 A100 T117 A140 K170 Y193 V196
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003974 UDP-N-acetylglucosamine 4-epimerase activity
GO:0016853 isomerase activity
Biological Process
GO:0009243 O antigen biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3rue, PDBe:3rue, PDBj:3rue
PDBsum3rue
PubMed
UniProtQ7BJX9|GNE_PLESH UDP-N-acetylglucosamine 4-epimerase (Gene Name=wbgU)

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