Structure of PDB 1vgv Chain B

Receptor sequence
>1vgvB (length=372) Species: 562 (Escherichia coli) [Search protein sequence]
MKVLTVFGTRPEAIKMAPLVHALAKDPFFEAKVCVTAQHREMLDQVLKLF
SIVPDYDLNIQGLTEITCRILEGLKPILAEFKPDVVLVHGDTTTTLATSL
AAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGHLAMYHFSPTETSRQ
NLLRENVADSRIFITGNTVIDALLWVRDQVMSSDKLRSELAANYPFIDPD
KKMILVTGHRRESFGRGFEEICHALADIATTHQDIQIVYPVHLNPNVREP
VNRILGHVKNVILIDPQEYLPFVWLMNHAWLILTDSGGIQEEAPSLGKPV
LVMRDTTERPEAVTAGTVRLVGTDKQRIVEEVTRLLKDENEYQAMSRAHN
PYGDGQACSRILEALKNNRISL
3D structure
PDB1vgv Structural analysis of a set of proteins resulting from a bacterial genomics project
ChainB
Resolution2.31 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D95 E117 E131 H213 R215 H246
Catalytic site (residue number reindexed from 1) D91 E113 E127 H209 R211 H242
Enzyme Commision number 5.1.3.14: UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing).
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 UD1 B R10 P11 H93 D95 E117 E131 H213 Q271 Y273 F276 S290 G292 E296 R313 R10 P11 H89 D91 E113 E127 H209 Q267 Y269 F272 S286 G288 E292 R309
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008761 UDP-N-acetylglucosamine 2-epimerase activity
GO:0016853 isomerase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0009246 enterobacterial common antigen biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1vgv, PDBe:1vgv, PDBj:1vgv
PDBsum1vgv
PubMed16021622
UniProtP27828|WECB_ECOLI UDP-N-acetylglucosamine 2-epimerase (Gene Name=wecB)

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