Structure of PDB 3c4v Chain A

Receptor sequence
>3c4vA (length=393) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
MRVAMISMHTSPLQQPGTGDSGGMNVYILSTATELAKQGIEVDIYTRATR
PSQGEIVRVAENLRVINIAAGPYEGLSKEELPTQLAAFTGGMLSFTRREK
VTYDLIHSHYWLSGQVGWLLRDLWRIPLIHTAHTLAAVDTPESEARRICE
QQLVDNADVLAVNTQEEMQDLMHHYDADPDRISVVSPGADVELYSPGNDR
ATERSRRELGIPLHTKVVAFVGRLQPFKGPQVLIKAVAALFDRDPDRNLR
VIICGGPTYRHMAEELGVEKRIRFLDPRPPSELVAVYRAADIVAVPSFNE
SFGLVAMEAQASGTPVIAARVGGLPIAVAEGETGLLVDGHSPHAWADALA
TLLDDDETRIRMGEDAVEHARTFSWAATAAQLSSLYNDAIANE
3D structure
PDB3c4v Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum: SUBSTRATE-ASSISTED CATALYSIS
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.250: D-inositol-3-phosphate glycosyltransferase.
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 R304 A306 T330 R288 A290 T314
BS02 UDP A Q15 P16 G22 G23 V229 R231 K236 C262 P293 R294 L299 E316 L320 V321 E324 Q15 P16 G22 G23 V221 R223 K228 C254 P277 R278 L283 E300 L304 V305 E308
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008375 acetylglucosaminyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
GO:0046872 metal ion binding
GO:0102710 D-inositol-3-phosphate glycosyltransferase activity
Biological Process
GO:0010125 mycothiol biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3c4v, PDBe:3c4v, PDBj:3c4v
PDBsum3c4v
PubMed18390549
UniProtQ8NTA6|MSHA_CORGL D-inositol 3-phosphate glycosyltransferase (Gene Name=mshA)

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