Structure of PDB 1f6d Chain D

Receptor sequence
>1f6dD (length=374) Species: 562 (Escherichia coli) [Search protein sequence]
MKVLTVFGTRPEAIKMAPLVHALAKDPFFEAKVCVTAQHREMLDQVLKLF
SIVPDYDLNIMQPGQGLTEITCRILEGLKPILAEFKPDVVLVHGDTTTTL
ATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGHLAMYHFSPTE
TSRQNLLRENVADSRIFITGNTVIDALLWVRDQVMSSDKLRSELAANYPF
IDPDKKMILVTGHRRESFGRGFEEICHALADIATTHQDIQIVYPVHLNPN
VREPVNRILGHVKNVILIDPQEYLPFVWLMNHAWLILTDSGGIQEEAPSL
GKPVLVMRDTTERPEAVTAGTVRLVGTDKQRIVEEVTRLLKDENEYQAMS
RAHNPYGDGQACSRILEALKNNRI
3D structure
PDB1f6d The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases.
ChainD
Resolution2.5 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) D95 E117 E131 H213 R215 H246
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 UDP D Q271 Y273 F276 G292 E296 Q271 Y273 F276 G292 E296
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:1f6d, PDBe:1f6d, PDBj:1f6d
PDBsum1f6d
PubMed11106477
UniProtP27828|WECB_ECOLI UDP-N-acetylglucosamine 2-epimerase (Gene Name=wecB)

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