Structure of PDB 1ek6 Chain B

Receptor sequence
>1ek6B (length=345) Species: 9606 (Homo sapiens) [Search protein sequence]
AEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRR
VQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKP
LDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTG
GCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDP
QGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGH
IAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARRE
GDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGT
3D structure
PDB1ek6 Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.
ChainB
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S132 A133 T134 Y157 K161
Catalytic site (residue number reindexed from 1) S131 A132 T133 Y156 K160
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
5.1.3.7: UDP-N-acetylglucosamine 4-epimerase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003974 UDP-N-acetylglucosamine 4-epimerase activity
GO:0003978 UDP-glucose 4-epimerase activity
GO:0016853 isomerase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006012 galactose metabolic process
GO:0019388 galactose catabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:1ek6, PDBe:1ek6, PDBj:1ek6
PDBsum1ek6
PubMed10801319
UniProtQ14376|GALE_HUMAN UDP-glucose 4-epimerase (Gene Name=GALE)

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