Structure of PDB 3o3p Chain A

Receptor sequence
>3o3pA (length=318) Species: 49319 (Rubrobacter xylanophilus) [Search protein sequence]
GPASAAEWFRQRSYDYGQFPPEDLARRKRELGLTVSAVLPSRNVADTVGG
IIDEIHALNERAPLIDQILVVDADSEDGTAGVAASHGAEVYSENELMSGY
GDAHGKGDAMWRALSVTRGDLVLYIDADTRDFRPQLAYGVLGPVLEVPGV
RFVKAAYRRPEEDGGGRVTELTAKPLFNLFYPELAGFVQPLAGEFVADRE
LFCSIPFLTGYAVETGIMIDVLKKVGLGAMAQVDLGERQNRHQHLRDLSR
MSYAVVRAVARRLRQEGRLQQLREPGLPESFFQLSDYLHAVATPEGLKLQ
EYVEELVERPPINEVLRV
3D structure
PDB3o3p Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity
ChainA
Resolution2.529 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P72 T231 Q248 E253 R254
Catalytic site (residue number reindexed from 1) P63 T215 Q232 E237 R238
Enzyme Commision number 2.4.1.266: glucosyl-3-phosphoglycerate synthase.
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 Q299 D302 Q283 D286
BS02 MG A D137 N256 D128 N240
BS03 GDD A P49 S50 R51 A82 E102 G114 K115 D135 A136 L207 G209 Y227 E230 N256 Q259 P40 S41 R42 A73 E93 G105 K106 D126 A127 L191 G193 Y211 E214 N240 Q243
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
GO:0050504 mannosyl-3-phosphoglycerate synthase activity

View graph for
Molecular Function
External links
PDB RCSB:3o3p, PDBe:3o3p, PDBj:3o3p
PDBsum3o3p
PubMed21166895
UniProtB7SY86

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