BioLiP

Structure of PDB 2x86 Chain S

Receptor sequence

>2x86S (length=307) Species: 562 (Escherichia coli) [Search protein sequence]

MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADY
MDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKEL
LHYCLEREIPFLYASSAATYGGRTSDFIESREYEKPLNVFGYSKFLFDEY
VRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKL
FEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADAT
LAYHKKGQIEYIPFPDKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVT
EYMAWLN

3D structure

PDB

2x86 The Crystal Structure of the Y140F Mutant of Adp-L-Glycero-D-Manno-Heptose 6-Epimerase Bound to Adp-Beta-D-Mannose Suggests a One Base Mechanism.

Chain

Resolution

2.8 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	S80 S116 F140 K144 K178 H187 Q277 N282 L283
Catalytic site (residue number reindexed from 1)	S80 S116 F140 K144 K178 H187 Q277 N282 L283
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)
BS01	NAP	S	G6 G9 F10 I11 D31 N32 K38 K53 E75 G76 A77 Y88 N92 Y96 A114 S116 F140 K144 Y167 V170 H177 K178	G6 G9 F10 I11 D31 N32 K38 K53 E75 G76 A77 Y88 N92 Y96 A114 S116 F140 K144 Y167 V170 H177 K178
BS02	ADP	S	N169 S180 M181 A182 V184 H187 F201 R209 F243 Y272	N169 S180 M181 A182 V184 H187 F201 R209 F243 Y272
BS03	BMA	S	S79 K178	S79 K178

Gene Ontology

	Molecular Function
GO:0008712	ADP-glyceromanno-heptose 6-epimerase activity
GO:0016853	isomerase activity
GO:0050661	NADP binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0009244	lipopolysaccharide core region biosynthetic process
GO:0097171	ADP-L-glycero-beta-D-manno-heptose biosynthetic process

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Molecular Function

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Biological Process

PDB	RCSB:2x86, PDBe:2x86, PDBj:2x86
PDBsum	2x86
PubMed	20506248
UniProt	P67911\|HLDD_ECO57 ADP-L-glycero-D-manno-heptose-6-epimerase (Gene Name=hldD)