Structure of PDB 5cgm Chain A

Receptor sequence
>5cgmA (length=669) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
GSVAGRIVIDDVQPVVSNGRYPAKAVVGEVVPVAATVWREGHDAVAATLV
VRYHGTTYPDLADPPPGPQRLPMSPGHTPDVFHGHFTPDRVGLWTYRVDG
WGDPIASWRHNVTAKLQGESELNNDLLVGARLLERAATGVPRELREALLE
AAAALRAPGDPFTRAGAALSAEVSDLLAEYPLREFVTRGEQYGVWVDRPE
ARFSSWYEMFPRSTGGWDAEGRPVHGTFATAAEALPRIARMGFDVVYLPP
IHPIGKVHRKGRNNSVTAAPGDVGSPWAIGSDEGGHDAVHPQLGTIEDFD
EFVASARDLGLEVALDLALQCAPDHPWAREHPEWFTVLPDGSIAYAEKYQ
DIYPLNFDNDPAGIYQEVLRVVRFWISHGVNIFRVDNPHTKPPNFWAWLI
GQIKNENPDVLFLSEAFTRPARLYGLAKLGFTQSYTYFTWRTSKWELTEF
GQEIAAKADIARPNLFVNTPDILHESLQHGGPGMFAIRAVLAATMGPAWG
VYSGYELFENQPVRPGSEEYLNSEKYELRPRDFESALARGESLEPFLTRL
NEIRRLHPALRELRTIRFHHVDNDALLAYSKFDPGTGDTVLVVVTLNPFG
AEEATLWLDMPELGMEPYDRFWVRDEITGEEYQWGQANYVRLDPAKAVAH
VLNMPLIPADKRLQLLRRE
3D structure
PDB5cgm Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.
ChainA
Resolution1.95 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 A W300 Q343 Y376 R411 D413 E442 D498 W277 Q320 Y349 R384 D386 E415 D471
BS02 GLC A K283 S298 W300 Y376 D378 K552 Y553 K260 S275 W277 Y349 D351 K525 Y526
BS03 PO4 A G96 H97 T98 H103 R694 E696 G76 H77 T78 H83 R667 E669
BS04 PO4 A T445 R446 R449 T418 R419 R422
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:5cgm, PDBe:5cgm, PDBj:5cgm
PDBsum5cgm
PubMed26616850
UniProtG7CL00

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