Structure of PDB 2x86 Chain D

Receptor sequence

>2x86D (length=307) Species: 562 (Escherichia coli)

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: D
• Resolution: 2.8 Å

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)	Binding affinity
BS01	NAP	D	G6 G9 F10 I11 D31 N32 K38 K53 E75 G76 A77 C78 S79 N92 Y96 A114 S116 F140 K144 Y167 V170 H177 K178	G6 G9 F10 I11 D31 N32 K38 K53 E75 G76 A77 C78 S79 N92 Y96 A114 S116 F140 K144 Y167 V170 H177 K178
BS02	ADP	D	S180 M181 V184 H187 L200 F201 R209 F243 Y272	S180 M181 V184 H187 L200 F201 R209 F243 Y272
BS03	BMA	D	S79 S116 F140 K178 M181	S79 S116 F140 K178 M181

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

External links

• 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)