Structure of PDB 1a9z Chain A

Receptor sequence
>1a9zA (length=338) Species: 562 (Escherichia coli) [Search protein sequence]
MRVLVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGK
HPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNN
VNGTLRLISAMRAANVKNFIFSSAATVYGDNPKIPYVESFPTGTPQSPFG
KSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNL
MPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKL
ANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYW
ADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
3D structure
PDB1a9z Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A124 A125 T126 F149 K153
Catalytic site (residue number reindexed from 1) A124 A125 T126 F149 K153
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003978 UDP-glucose 4-epimerase activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
GO:0042802 identical protein binding
GO:0070403 NAD+ binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006012 galactose metabolic process
GO:0009242 colanic acid biosynthetic process
GO:0033499 galactose catabolic process via UDP-galactose
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:1a9z, PDBe:1a9z, PDBj:1a9z
PDBsum1a9z
PubMed9708982
UniProtP09147|GALE_ECOLI UDP-glucose 4-epimerase (Gene Name=galE)

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