Structure of PDB 1eq2 Chain I

Receptor sequence
>1eq2I (length=307) Species: 562 (Escherichia coli) [Search protein sequence]
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADY
MDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKEL
LHYCLEREIPFLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEY
VRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKL
FEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADAT
LAYHKKGQIEYIPFPDKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVT
EYMAWLN
3D structure
PDB1eq2 The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.
ChainI
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S116 Y140 K144 K178
Catalytic site (residue number reindexed from 1) S116 Y140 K144 K178
Enzyme Commision number 5.1.3.20: ADP-glyceromanno-heptose 6-epimerase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008712 ADP-glyceromanno-heptose 6-epimerase activity
GO:0016853 isomerase activity
GO:0050661 NADP binding
GO:0070401 NADP+ binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009244 lipopolysaccharide core region biosynthetic process
GO:0097171 ADP-L-glycero-beta-D-manno-heptose biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:1eq2, PDBe:1eq2, PDBj:1eq2
PDBsum1eq2
PubMed10896473
UniProtP67910|HLDD_ECOLI ADP-L-glycero-D-manno-heptose-6-epimerase (Gene Name=hldD)

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