Structure of PDB 1lrk Chain A

Receptor sequence
>1lrkA (length=338) Species: 562 (Escherichia coli) [Search protein sequence]
MRVLVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGK
HPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNN
VNGTLRLISAMRAANVKNFIFSSSATVYGDNPKIPYVESFPTGTPQSPYG
KSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNL
MPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKL
ANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPACW
ADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
3D structure
PDB1lrk Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks.
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S124 A125 T126 Y149 K153 M189
Catalytic site (residue number reindexed from 1) S124 A125 T126 Y149 K153 M189
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1lrk, PDBe:1lrk, PDBj:1lrk
PDBsum1lrk
PubMed12019271
UniProtP09147|GALE_ECOLI UDP-glucose 4-epimerase (Gene Name=galE)

[Back to BioLiP]