Structure of PDB 3c4q Chain B

Receptor sequence
>3c4qB (length=393) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
MRVAMISMHTSPLQQPGTGDSGGMNVYILSTATELAKQGIEVDIYTRATR
PSQGEIVRVAENLRVINIAAGPYEGLSKEELPTQLAAFTGGMLSFTRREK
VTYDLIHSHYWLSGQVGWLLRDLWRIPLIHTAHTLAAVSDTPESEARRIC
EQQLVDNADVLAVNTQEEMQDLMHHYDADPDRISVVSPGADVELYSPGND
RATERSRRELGIPLHTKVVAFVGRLQPFKGPQVLIKAVAALFDRDPDRNL
RVIICGGPYRHMAEELGVEKRIRFLDPRPPSELVAVYRAADIVAVPSFNE
SFGLVAMEAQASGTPVIAARVGGLPIAVAEGETGLLVDGHSPHAWADALA
TLLDDDETRIRMGEDAVEHARTFSWAATAAQLSSLYNDAIANE
3D structure
PDB3c4q Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum: SUBSTRATE-ASSISTED CATALYSIS
ChainB
Resolution2.8 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 B Y303 R304 A306 T330 Y287 R288 A290 T314
BS02 UDP B Q15 P16 G23 V229 R231 K236 P293 R294 L299 L320 V321 E324 Q15 P16 G23 V222 R224 K229 P277 R278 L283 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:3c4q, PDBe:3c4q, PDBj:3c4q
PDBsum3c4q
PubMed18390549
UniProtQ8NTA6|MSHA_CORGL D-inositol 3-phosphate glycosyltransferase (Gene Name=mshA)

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