Structure of PDB 2hxu Chain A

Receptor sequence
>2hxuA (length=434) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
RTIIALETHDVRFPTSRELDGSDAMNPDPDYSAAYVVLRTDGAEDLAGYG
LVFTIGRGNDVQTAAVAALAEHVVGLSVDKVIADLGAFARRLTNDSQLRW
LGPEKGVMHMAIGAVINAAWDLAARAANKPLWRFIAELTPEQLVDTIDFR
YLSDALTRDEALAILRDAQPQRAARTATLIEQGYPAYTTSPGWLGYSDEK
LVRLAKEAVADGFRTIKLAVGANVQDDIRRCRLARAAIGPDIAMAVDANQ
RWDVGPAIDWMRQLAEFDIAWIEEPTSPDDVLGHAAIRQGITPVPVSTGE
HTQNRVVFKQLLQAGAVDLIQIDAARVGGVNENLAILLLAAKFGVRVFPH
AGGVGLCELVQHLAMADFVAITGKMEDRAIEFVDHLHQHFLDPVRIQHGR
YLAPEVPGFSAEMHPASIAEFSYPDGRFWVEDLA
3D structure
PDB2hxu Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas campestris.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T55 T190 K218 A220 D248 N250 E274 G300 E301 D324 P350 H351 A352 D368 K375 E382
Catalytic site (residue number reindexed from 1) T54 T189 K217 A219 D247 N249 E273 G299 E300 D323 P349 H350 A351 D367 K374 E381
Enzyme Commision number 4.2.1.68: L-fuconate dehydratase.
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 MG A D248 E274 E301 D247 E273 E300
BS02 LFC A G22 D24 Y32 W194 K218 D248 E301 H351 G353 E382 G21 D23 Y31 W193 K217 D247 E300 H350 G352 E381
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:0050023 L-fuconate dehydratase activity
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2hxu, PDBe:2hxu, PDBj:2hxu
PDBsum2hxu
PubMed17144652
UniProtQ8P3K2|FUCD_XANCP L-fuconate dehydratase (Gene Name=XCC4069)

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