Structure of PDB 3kia Chain C

Receptor sequence
>3kiaC (length=308) Species: 32630 (synthetic construct) [Search protein sequence]
LGPASAAEWFRQRSYDYGQFPPEDLARRKRELGLTVSAVLPSRNVADTVG
GIIDEIHALNERAPLIDQILVVDADSEDGTAGVAASHGAEVYSENELMSG
YGDAHGKGDAMWRALSVTRGDLVLYIDADTRDFRPQLAYGVLGPVLEVPG
VRFVKAAYRRPEDGGGRVTELTAKPLFNLFYPELAGFVQPLAGEFVADRE
LFCSIPFLTGYAVETGIMIDVLKKVGLGAMAQVDLGERQNRHLRDLSRMS
YAVVRAVARRLRQEGRLQQLSFFQLSDYLHAVATPEGLKLQEYVEELVER
PPINEVLR
3D structure
PDB3kia Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity
ChainC
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) P72 T231 Q248 E253 R254
Catalytic site (residue number reindexed from 1) P64 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 5GP C P49 S50 R51 E102 G114 K115 D135 A136 D137 Y227 P41 S42 R43 E94 G106 K107 D127 A128 D129 Y211
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:3kia, PDBe:3kia, PDBj:3kia
PDBsum3kia
PubMed21166895
UniProtB7SY86

[Back to BioLiP]