Structure of PDB 5cim Chain B

Receptor sequence
>5cimB (length=675) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
SVAGRIVIDDVQPVVSNGRYPAKAVVGEVVPVAATVWREGHDAVAATLVV
RYHGTTYPDLADPPPGVPGAVKPQRLPMSPGHTPDVFHGHFTPDRVGLWT
YRVDGWGDPIASWRHNVTAKLSELNNDLLVGARLLERAATGVPRELREAL
LEAAAALRAPGDPFTRAGAALSAEVSDLLAEYPLREFVTRGEQYGVWVDR
PEARFSSWYEMFPRSTGGWDAEGRPVHGTFATAAEALPRIARMGFDVVYL
PPIHPIGKVHRKGRNNSVTAAPGDVGSPWAIGSDEGGHDAVHPQLGTIED
FDEFVASARDLGLEVALDLALQCAPDHPWAREHPEWFTVLPDGSIAYAEN
PPKKYQDIYPLNFDNDPAGIYQEVLRVVRFWISHGVNIFRVDNPHTKPPN
FWAWLIGQIKNENPDVLFLSEAFTRPARLYGLAKLGFTQSYTYFTWRTSK
WELTEFGQEIAAKADIARPNLFVNTPDILHESLQHGGPGMFAIRAVLAAT
MGPAWGVYSGYELFENQPVRPGSEEYLNSEKYELRPRDFESALARGESLE
PFLTRLNEIRRLHPALRELRTIRFHHVDNDALLAYSKFDPGTGDTVLVVV
TLNPFGAEEATLWLDMPELGMEPYDRFWVRDEITGEEYQWGQANYVRLDP
AKAVAHVLNMPLIPADKRLQLLRRE
3D structure
PDB5cim Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.
ChainB
Resolution3.32 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.99.16: starch synthase (maltosyl-transferring).
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 GLC B Q343 R411 D413 E442 D498 K552 Q322 R390 D392 E421 D477 K531
BS02 GLC B K283 S298 W300 Y376 D378 I379 K552 Y553 K262 S277 W279 Y355 D357 I358 K531 Y532
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030979 alpha-glucan biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5cim, PDBe:5cim, PDBj:5cim
PDBsum5cim
PubMed26616850
UniProtG7CL00

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