Structure of PDB 1i8t Chain B

Receptor sequence
>1i8tB (length=367) Species: 562 (Escherichia coli) [Search protein sequence]
MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQI
HKYGAHIFHTNDKYIWDYVNDLVEFNRFTNSPLAIYKDKLFNLPFNMNTF
HQMWGVKDPQEAQNIINAQKKKYGDKVPENLEEQAISLVGEDLYQALIKG
YTEKQWGRSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEK
MLEGVDVKLGIDFLKDKDSLASKAHRIIYTGPIDQYFDYRFGALEYRSLK
FETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYP
LEWKVGDEPYYPVNDNKNMELFKKYRELASREDKVIFGGRLAEYKYYDMH
QVISAALYQVKNIMSTD
3D structure
PDB1i8t UDP-galactopyranose mutase has a novel structure and mechanism.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R170 R174 R247 R278 E298 Y346 D348
Catalytic site (residue number reindexed from 1) R170 R174 R247 R278 E298 Y346 D348
Enzyme Commision number 5.4.99.9: UDP-galactopyranose mutase.
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 FAD B V7 G8 G10 F12 E31 K32 G38 N39 A55 H56 I57 D212 F213 G231 Y311 G339 R340 Y346 Y347 D348 M349 V7 G8 G10 F12 E31 K32 G38 N39 A55 H56 I57 D212 F213 G231 Y311 G339 R340 Y346 Y347 D348 M349
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008767 UDP-galactopyranose mutase activity
GO:0016853 isomerase activity
GO:0042803 protein homodimerization activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009103 lipopolysaccharide biosynthetic process
Cellular Component
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:1i8t, PDBe:1i8t, PDBj:1i8t
PDBsum1i8t
PubMed11573090
UniProtP37747|GLF_ECOLI UDP-galactopyranose mutase (Gene Name=glf)

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