Structure of PDB 1eq2 Chain E

Receptor sequence
>1eq2E (length=300) Species: 562 (Escherichia coli) [Search protein sequence]
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADY
MDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKEL
LHYCLEREIPFLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEY
VRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKL
FEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADAT
LAYHKKGQIEYIPFYQAFTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLN
3D structure
PDB1eq2 The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.
ChainE
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
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 NAP E G6 G9 F10 I11 D31 N32 K38 K53 E75 G76 A77 S79 N92 Y96 A114 S116 Y140 K144 Y167 V170 H177 K178 G6 G9 F10 I11 D31 N32 K38 K53 E75 G76 A77 S79 N92 Y96 A114 S116 Y140 K144 Y167 V170 H177 K178
BS02 ADQ E S180 V184 H187 F201 R209 F243 S180 V184 H187 F201 R209 F243
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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Biological Process

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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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