Structure of PDB 1n7h Chain A

Receptor sequence

>1n7hA (length=331) Species: 3702 (Arabidopsis thaliana)

RKIALITGITGQDGSYLTEFLLGKGYEVHGLIRRSSNFNTQRINHIYALM
KLHYADLTDASSLRRWIDVIKPDEVYNLAAQSHVAVSFEIPDYTADVVAT
GALRLLEAVRSHTIDSGRTVKYYQAGSSEMFGSTPPPQSETTPFHPRSPY
AASKCAAHWYTVNYREAYGLFACNGILFNHESPRRGENFVTRKITRALGR
IKVGLQTKLFLGNLQASRDWGFAGDYVEAMWLMLQQEKPDDYVVATEEGH
TVEEFLDVSFGYLGLNWKDYVEIDQRYFRPAEVDNLQGDASKAKEVLGWK
PQVGFEKLVKMMVDEDLELAKREKVLVDAGY

3D structure

• PDB: 1n7h The structure of the MUR1 GDP-mannose 4,6-dehydratase from A. thaliana: Implications for ligand binding and specificity.
• Chain: A
• Resolution: 1.8 Å

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	A	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
BS02	GDP	A	N214 F224 V225 K228 L246 G247 N248 R253 R314 E317	N179 F189 V190 K193 L211 G212 N213 R218 R279 E282

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

External links

• PDB: RCSB:1n7h, PDBe:1n7h, PDBj:1n7h
• PDBsum: 1n7h
• PubMed: 12501186
• UniProt: P93031|GMD2_ARATH GDP-mannose 4,6 dehydratase 2 (Gene Name=MUR1)