Structure of PDB 2hne Chain A

Receptor sequence
>2hneA (length=426) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
MRTIIALETHDVRFPTSREPDPDYSAAYVVLRTDGAEDLAGYGLVFTIGR
GNDVQTAAVAALAEHVVGLSVDKVIADLGAFARRLTNDSQLRWLGPEKGV
MHMAIGAVINAAWDLAARAANKPLWRFIAELTPEQLVDTIDFRYLSDALT
RDEALAILRDAQPQRAARTATLIEQGYPAYTTSPGWLGYSDEKLVRLAKE
AVADGFRTIKLKVGANVQDDIRRCRLARAAIGPDIAMAVDANQRWDVGPA
IDWMRQLAEFDIAWIEEPTSPDDVLGHAAIRQGITPVPVSTGEHTQNRVV
FKQLLQAGAVDLIQIDAARVGGVNENLAILLLAAKFGVRVFPHAGGVGLC
ELVQHLAMADFVAITGKMEDRAIEFVDHLHQHFLDPVRIQHGRYLAPEVP
GFSAEMHPASIAEFSYPDGRFWVEDL
3D structure
PDB2hne Crystal structure of l-fuconate dehydratase from xanthomonas campestris pv. campestris str. ATCC 33913
ChainA
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) T55 T190 K218 K220 D248 N250 E274 G300 E301 D324 P350 H351 A352 D368 K375 E382
Catalytic site (residue number reindexed from 1) T47 T182 K210 K212 D240 N242 E266 G292 E293 D316 P342 H343 A344 D360 K367 E374
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 D240 E266 E293
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:2hne, PDBe:2hne, PDBj:2hne
PDBsum2hne
PubMed
UniProtQ8P3K2|FUCD_XANCP L-fuconate dehydratase (Gene Name=XCC4069)

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