Structure of PDB 1n7g Chain D

Receptor sequence
>1n7gD (length=313) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
RKIALITGITGQDGSYLTEFLLGKGYEVHGLIRRSSNFNTQRINHIYILM
KLHYADLTDASSLRRWIDVIKPDEVYNLAAQSHVAVSFEIPDYTADVVAT
GALRLLEAVRSHTIDSGRTVKYYQAGSSEMFGSTPPPQSETTPFHPRSPY
AASKCAAHWYTVNYREAYGLFACNGILFNHESPRRGENFVTRKITRALGR
IKVGLQTKLFASRDWGFAGDYVEAMWLMLQQEKPDDYVVATEEGHTVEEF
LDVSFGYLGLNWKDYVEIDDNLQGDASKAKEVLGWKPQVGFEKLVKMMVD
EDLELAKREKVLV
3D structure
PDB1n7g The structure of the MUR1 GDP-mannose 4,6-dehydratase from A. thaliana: Implications for ligand binding and specificity.
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S162 S163 E164 Y185 K189
Catalytic site (residue number reindexed from 1) S127 S128 E129 Y150 K154
Enzyme Commision number 4.2.1.47: GDP-mannose 4,6-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 NDP D R61 S62 S63 R34 S35 S36
BS02 NDP D G35 T37 G38 Q39 D40 R60 D91 L92 L113 A114 A115 S117 A160 G161 S162 Y185 K189 L212 N214 H215 R220 G8 T10 G11 Q12 D13 R33 D56 L57 L78 A79 A80 S82 A125 G126 S127 Y150 K154 L177 N179 H180 R185
Gene Ontology
Molecular Function
GO:0005525 GTP binding
GO:0008446 GDP-mannose 4,6-dehydratase activity
GO:0016829 lyase activity
Biological Process
GO:0009826 unidimensional cell growth
GO:0019673 GDP-mannose metabolic process
GO:0042350 GDP-L-fucose biosynthetic process
GO:0042351 'de novo' GDP-L-fucose biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1n7g, PDBe:1n7g, PDBj:1n7g
PDBsum1n7g
PubMed12501186
UniProtP93031|GMD2_ARATH GDP-mannose 4,6 dehydratase 2 (Gene Name=MUR1)

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