Structure of PDB 3o3p Chain A Binding Site BS02
Receptor Information
>3o3p Chain A (length=318) Species:
49319
(Rubrobacter xylanophilus) [
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GPASAAEWFRQRSYDYGQFPPEDLARRKRELGLTVSAVLPSRNVADTVGG
IIDEIHALNERAPLIDQILVVDADSEDGTAGVAASHGAEVYSENELMSGY
GDAHGKGDAMWRALSVTRGDLVLYIDADTRDFRPQLAYGVLGPVLEVPGV
RFVKAAYRRPEEDGGGRVTELTAKPLFNLFYPELAGFVQPLAGEFVADRE
LFCSIPFLTGYAVETGIMIDVLKKVGLGAMAQVDLGERQNRHQHLRDLSR
MSYAVVRAVARRLRQEGRLQQLREPGLPESFFQLSDYLHAVATPEGLKLQ
EYVEELVERPPINEVLRV
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
3o3p Chain A Residue 339 [
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Receptor-Ligand Complex Structure
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PDB
3o3p
Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity
Resolution
2.529 Å
Binding residue
(original residue number in PDB)
D137 N256
Binding residue
(residue number reindexed from 1)
D128 N240
Annotation score
1
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.
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
PDBsum
3o3p
PubMed
21166895
UniProt
B7SY86
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